Difference between revisions of "User talk:Z3417843"

From CellBiology
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13.16374451
 
13.16374451
 
14.15205311
 
14.15205311
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{| class="wikitable"
 +
|-
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! Laminin Heterotrimer!! Function
 +
|-
 +
| <center>'''Laminin-111'''</center> || <center>involved in regulating muscular morphogenesis by promoting regeneration in muscle cells<ref name="PMID25015639"><pubmed>25015639</pubmed></ref><ref name="PMID24009313"><pubmed>24009313</pubmed></ref>; promotes neurite outgrowth in human mesenchymal cells via activation of FAK and MAPK cascades<ref name="PMID19895795"><pubmed>19895795</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-211'''</center> || <center>essential for the contractility of airway smooth muscle cells<ref name="PMID23756649"><pubmed>23756649</pubmed></ref><ref name="PMID19213874"><pubmed>19213874</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-121'''</center> || <center>has a strong affinity for α7β1 integrin, which promotes neurite outgrowth <ref name="PMID20566382"><pubmed>20566382</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-221'''</center> || <center></center>
 +
|-
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| <center>'''Laminin-332'''</center> || <center>involved in the synthesis of tyrosine, which increase the level of melanin produced by melanocytes<ref name="PMID24951591"><pubmed>24951591</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-311'''</center> || <center>involved in the maintenance of the alveolar tissue architecture <ref name="PMID16714422"><pubmed>16714422</pubmed></ref></center>
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|-
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| <center>'''Laminin-321'''</center> || <center></center>
 +
|-
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| <center>'''Laminin-411'''</center> || <center>has a vascular role; increases the migration and adhesion of human dermal microvascular endothelial cells (HDMECs), which promote the tubule formation of endothelial cells<ref name="PMID16374451"><pubmed>16374451</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-421'''</center> || <center></center>
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|-
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| <center>'''Laminin-511'''</center> || <center>a potent substrate for up regulating α3β1, which is a promoter for hair growth<ref name="PMID20211547"><pubmed>20211547</pubmed></ref><ref name="PMID12743034"><pubmed>12743034</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-521'''</center> || <center>essential for the formation of the glomerular filtration barrier (as reviewed in <ref name="PMID21519194><pubmed>21519194</pubmed></ref>; also involved in preventing Schwann cells from invading the synaptic cleft in a neuromuscular junction <ref name="PMID21766463"><pubmed>21766463</pubmed></ref></center>
 +
|-
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| <center>'''Laminin-213'''</center> || <center></center>
 +
|-
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| <center>'''Laminin-423'''</center> || <center></center>
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|-
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| <center>'''Laminin-522'''</center> || <center></center>
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|-
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| <center>'''Laminin-523'''</center> || <center></center>
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|}
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 +
{| class="wikitable mw-collapsible mw-collapsed"
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! Laminin 111
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|-
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|
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{|
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|-bgcolor="F5FFFA"
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|
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Laminin 111 (LM-111) is the one of the first, and predominant, ECM proteins expressed during embryonic development<ref name="PMID25015639"><pubmed>25015639</pubmed></ref><ref name="PMID24706882"><pubmed>24706882</pubmed></ref>. LM-111 provides structural support to the BM<ref name="PMID24706882"><pubmed>24706882</pubmed></ref>. More importantly, this LM isoform’s main role is to regulate muscular regeneration<ref name="PMID25015639"><pubmed>25015639</pubmed></ref><ref name="PMID24009313"><pubmed>24009313</pubmed></ref>.  LM-111 is known to prevent the effects of muscular dystrophy, such as skeletal muscle weakness due to damages in cells and tissues<ref name="PMID25015639"><pubmed>25015639</pubmed></ref><ref name="PMID24009313"><pubmed>24009313</pubmed></ref>. It does this by playing a role in myoblast fusion<ref name="PMID25015639"><pubmed>25015639</pubmed></ref>, the formation of new and larger myofibres, and acting as a substitute to LM-α2 deficiency<ref name="PMID24009313"><pubmed>24009313</pubmed></ref>. The injection of LM-111 helps re-establish the sarcolemma in muscle cells that are laminin-a2 deficient<ref name="PMID24009313"><pubmed>24009313</pubmed></ref>. This LM isoform also increases muscle integrity by interacting with a7B1 integrin and a-dystroglycan<ref name="PMID24009313"><pubmed>24009313</pubmed></ref>, which improves the number of satellite cells by improving satellite cell proliferation<ref name="PMID25015639"><pubmed>25015639</pubmed></ref><ref name="PMID24009313"><pubmed>24009313</pubmed></ref>. LM-111 provides a link between the ECM and the sarcolemma, which prevents muscle degeneration and apoptosis, and promotes muscular adhesion to the basal lamina<ref name="PMID24009313"><pubmed>24009313</pubmed></ref>. There is evidence showing that LM-111 prevents muscle damage. In postexercise mice, those that were treated with the laminin isoform had fewer muscle fibres with centrally located nuclei, which is commonly a sign for muscle damage<ref name="PMID25015639"><pubmed>25015639</pubmed></ref>.
 +
LM-111 also plays a role in the epithelial-to-mesenchymal transition (EMT) in cells. A fragment of the LM molecule interacts with matrix metalloproteinases (MMPs), specifically MMP2. The LM-111 fragment down-regulates MMP2, which in turn lowers the amount of BM undergoing degradation<ref name="PMID24706882"><pubmed>24706882</pubmed></ref>.
 +
|}
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|}
 +
{| class="wikitable mw-collapsible mw-collapsed"
 +
! Laminin 211
 +
|-
 +
|
 +
{|
 +
|-bgcolor="F5FFFA"
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|
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Laminin 211 (LM-211) plays a role in the contractility of airway smooth muscle (ASM) cells, which relates to the pathology of asthmatic attacks. The expression of this LM isoform in ASM cells is essential for its contractility as well as reducing the levels of proapoptotic proteins in ASM cells <ref name="PMID23756649"><pubmed>23756649</pubmed></ref><ref name="PMID19213874"><pubmed>19213874</pubmed></ref>, which results in the hypertrophy of these cells<ref name="PMID23756649"><pubmed>23756649</pubmed></ref>. This relates to asthma because asthmatic airways are characterised to have ASM cells with increased contractility<ref name="PMID19213874"><pubmed>19213874</pubmed></ref>.
 +
LM-211 also has a role in the control in the interactions between thymocytes and thymic epithelial cells (TECs). The deposit of LM-211 creates a microenvironment for thymocytes to proliferate, maturate, differentiate, and migrate. Furthermore, the thymocyte-TEC interaction was blocked when antibodies specific for LM-211 were introduced<ref name="PMID18644586"><pubmed>18644586</pubmed></ref>.
 +
|}
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|}
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{| class="wikitable mw-collapsible mw-collapsed"
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! Laminin 332
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|-
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|
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{|
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|-bgcolor="F5FFFA"
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|
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Melanocytes are cells that synthesise melanin, a component of the pigmentary system of the skin. The melanin, produced by melanocytes, migrate to keratinocytes for protection. Laminin 332 (LM-332) is derived from keratinocytes and plays a role in the migration and adhesion of melanocytes<ref name="PMID24951591"><pubmed>24951591</pubmed></ref><ref name="PMID21349841"><pubmed>21349841</pubmed></ref>. LM-332 is also promotes the synthesis of melanin in melanocytes by controlling the levels of tyrosine<ref name="PMID24951591"><pubmed>24951591</pubmed></ref>. Tyrosine is essential for the synthesis of melanin and it's level is proportional to the level of melanin i.e. an increase in the level of tyrosine will also increase the level of melanin made<ref name="PMID21349841"><pubmed>21349841</pubmed></ref>. This links to LM-332 because this LM isoform increases the intracellular tyrosine levels and also increases the uptake of extracellular tyrosine<ref name="PMID21349841"><pubmed>21349841</pubmed></ref>. However, the mechanism behind the control of tyrosine levels by LM-322 is still unknown.
 +
|}
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|}
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{| class="wikitable mw-collapsible mw-collapsed"
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! Laminin 411
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|-
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|
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{|
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|-bgcolor="F5FFFA"
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|
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Laminin 411 (LM-411) is expressed in the endothelial BM and plays a significant role in the maintenance of the vascular endothelial BM<ref name="PMID16374451"><pubmed>16374451</pubmed></ref>. Although, Laminin-511 maybe expressed in vascular endothelial BMs as well, LM-411 is expressed in all BMs of all blood vessels, whereas Laminin-511 is only expressed in capillaries and some veins and venules<ref name="PMID15205311"><pubmed>15205311</pubmed></ref>. This LM heterotrimer is involved in the survival of endothelial cells, particularly in their migration and adhesion<ref name="PMID16374451"><pubmed>16374451</pubmed></ref>. The presence of LM-411 increases the migration and adhesion of human dermal microvascular endothelial cells (HDMECs). In turn, the migration of HDMECs promotes tubule formation of endothelial cells<ref name="PMID16374451"><pubmed>16374451</pubmed></ref>. Therefore, it can be deduced that this laminin heterotrimer is involved in vascular formation. Therefore, a lack in LM-411 expression leads to disrupted vascular endothelial BMs. In a study, the lack of LM-411 expression resulted in a bleeding phenotype in newborn mice<ref name="PMID15205311"><pubmed>15205311</pubmed></ref>. LM-411 is related to type IV collage, in that the overexpression of LM-411 increases the number of type IV collagen in capillary BM. The absence of LM-411 leads to no formation of type IV collagen, which affects the assembly of the BM<ref name="PMID16374451"><pubmed>16374451</pubmed></ref>.
 +
 +
|}
 +
|}
 +
{| class="wikitable mw-collapsible mw-collapsed"
 +
! Laminin 511
 +
|-
 +
|
 +
{|
 +
|-bgcolor="F5FFFA"
 +
|
 +
Laminin 511 (LM-511) is one of the first ECM proteins expressed during embryogenesis<ref name="PMID25015639"><pubmed>25015639</pubmed></ref>. LM-511 is another LM heterotrimer, release by keratinocytes<ref name="PMID21067603"><pubmed>21067603</pubmed></ref>, associated with hair downgrowth<ref name="PMID16957169"><pubmed>16957169</pubmed></ref><ref name="PMID21067603"><pubmed>21067603</pubmed></ref>.  Lm-511 is found in the BMZ and interfollicular epithelia but it is most numerous in the BMZ, specifically around the hair follicles<ref name="PMID16957169"><pubmed>16957169</pubmed></ref>. Unlike LMm-332, LM-511 is the primary LM <ref name="PMID12743034"><pubmed>12743034</pubmed></ref> for the stimulation of hair growth and elongation<ref name="PMID20211547"><pubmed>20211547</pubmed></ref>. LM-511 is associated with α3 integrin, in terms of regulating hair growth<ref name="PMID16957169"><pubmed>16957169</pubmed></ref>. α3 integrin acts as a promoter of hair growth<ref name="PMID16957169"><pubmed>16957169</pubmed></ref>. This links back to LM-511, which is a potent substrate for the upregulation the expression of the α3β1 integrin<ref name="PMID20211547"><pubmed>20211547</pubmed></ref><ref name="PMID12743034"><pubmed>12743034</pubmed></ref><ref name="PMID21067603"><pubmed>21067603</pubmed></ref>. Therefore, the presence of LM-511 promotes hair growth via α3β1 integrins<ref name="PMID20211547"><pubmed>20211547</pubmed></ref><ref name="PMID12743034"><pubmed>12743034</pubmed></ref>. Another process as to how LM-511 affects hair follicle involves dermal blood vessels. α3 integrin is also involved in the migration of endothelial cells. Therefore, it is plausible that LM-511 is associated with the recruitment of dermal blood vessels essential for the formation of hair follicles<ref name="PMID12743034"><pubmed>12743034</pubmed></ref>. LM-511 is also involved in the formation of the BMZ. The lack of LM-511 results in a discontinuous lamina densa, which hinders the downgrowth of the hair follicles<ref name="PMID21067603"><pubmed>21067603</pubmed></ref>.
 +
 +
Together with LM-411, LM-511 also plays a role in the maintenance of the vascular endothelial BM<ref name="PMID15205311"><pubmed>15205311</pubmed></ref>. Unlike LM-411, LM-511 is expressed only in capillaries and some venules and veins. However, the failure to express LM-411 leads to compensation by LM-511. Due to this event, angiogenesis is increased, which conseuquently enhances the growth of tumours and finally metastasis. Therefore, this LM heterotrimer, even if not directly, is also involed in angiogenesis, tumour formation and metastasis<ref name="PMID15205311"><pubmed>15205311</pubmed></ref>.
 +
|}
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|}

Revision as of 11:21, 26 May 2015

Use this for working!

Laminin 332

Melanocytes are cells that synthesise melanin, a component of the pigmentary system of the skin. The melanin, produced by melanocytes, migrate to keratinocytes for protection. Laminin 332 (LM-332) is derived from keratinocytes and plays a role in the migration and adhesion of melanocytes (7,8). LM-332 is also promotes the synthesis of melanin in melanocytes by controlling the levels of tyrosine(7). Tyrosine is essential for the synthesis of melanin and it's level is proportional to the level of melanin i.e. an increase in the level of tyrosine will also increase the level of melanin made (8). This links to LM-332 because this laminin isoform increases the intracellular tyrosine levels and also increases the uptake of extracellular tyrosine(8). However, the mechanism behind the control of tyrosine levels by LM-322 is still unknown.

LM-332 is also involved in hair growth. This laminin isoform works with another laminin isoform, Laminin 511, in regulating the growth of hair follicles. Hemidesmosomes are structures found in the basement membrane. Hemidesmosomes prevent epidermal cells to move down into the connective tissue, which impedes hair growth. The presence of of LM-332 in the anagen stage leads to the loss of hemidesmosomes. Therefore, the loss of Lm-332 indirectly promotes hair growth (9).


Laminin 511

Laminin 511 (Lm-511) is another laminin heterotrimer, release by keratinocytes(12), associated with hair downgrowth. (12) Lm-511 is found in the basement membrane zone and interfollicular epithelia but it is most numerous in the basement membrane zone, specifically around the hair follicles. Unlike Lm-332, Lm-511 is the primary laminin (11) for the stimulation of hair growth and elongation (10). Lm-511 is associated with a3 integrin, in terms of regulating hair growth. a3 integrin acts as a promoter of hair growth. This links back to Lm-511, which is a potent substrate for the upregulation the expression of the a3B1 integrin(10,11,12). Therefore, the presence of Lm-511 promotes hair growth via a3B1 integrins (10,11). Another process as to how Lm-511 affects hair follicle involves dermal blood vessels. a3 integrin is also involved in the migration of endothelial cells. Therefore, it is plausible that Lm-511 is associated with the recruitment of dermal blood vessels essential for the formation of hair follicles(11). Lm-511 is also involved in the formation of the basement membrane zone. The lack of Lm-511 results in a discontinuous lamina densa, which hinders the downgrowth of the hair follicles. (12)

Together with Lm-411, Lm-511 also plays a role in the maintenance of the vascular endothelial basement membrane (14). Unlike Lm-411, Lm-511 is expressed only in capillaries and some venules and veins. However, the failure to express Lm-411 leads to compensation by Lm-511. In mice models, the bleeding phenotype was no longer visible at the same time as the expression of Lm-511.

Laminin 311

http://www.ncbi.nlm.nih.gov/pubmed/16714422 http://www.ncbi.nlm.nih.gov/pubmed/23209340

Laminin 411

Laminin 411 (Lm-411) is expressed in the endothelial basement membrane and plays a significant role in the maintenance of the vascular endothelial basement membrane. Although, Laminin-511 maybe expressed in vascular endothelial basement membranes as well, Lm-411 is expressed in all basement membranes of all blood vessels, whereas Laminin-511 is only expressed in capillaries and some veins and venules(14). This laminin heterotrimer is involved in the survival of endothelial cells, particularly in their migration and adhesion. The presence of Lm-411 increases the migration and adhesion of human dermal microvascular endothelial cells (HDMECs). In turn, the migration of HDMECs promotes tubule formation of endothelial cells. Therefore, it can be deduced that this laminin heterotrimer is involved in vascular formation. Therefore, a lack in Lm-411 expression leads to disrupted vascular endothelial basement membranes. In a study, the lack of Lm-411 expression resulted in a bleeding phenotype in newborn mice.(14) Lm-411 is related to type IV collage, in that the overexpression of Lm-411 increases the number of type IV collagen in capillary basement membrane. The absence of Lm-411 leads to no formation of type IV collagen, which affects the assembly of the basement membrane.

Together with Lm-411, Lm-511 also plays a role in the maintenance of the vascular endothelial basement membrane (14). Unlike Lm-411, Lm-511 is expressed only in capillaries and some venules and veins. However, the failure to express Lm-411 leads to compensation by Lm-511. Due to this event, angiogenesis is increased, which conseuquently enhances the growth of tumours and finally metastasis. Therefore, this laminin heterotrimer, even if not directly, is also involed in angiogenesis, tumour formation and metastasis. (14) http://www.ncbi.nlm.nih.gov/pubmed/17109197 http://www.ncbi.nlm.nih.gov/pubmed/16374451

http://www.ncbi.nlm.nih.gov/pubmed/15172971

References

1. 25015639 2. 24706882 3. 24009313 4. 18644586 5. 23756649 6. 19213874 7. 24951591 8. 21349841 9. 16957169 10.20211547 11.12743034 12.21067603 13.16374451 14.15205311


Laminin Heterotrimer Function
Laminin-111
involved in regulating muscular morphogenesis by promoting regeneration in muscle cells[1][2]; promotes neurite outgrowth in human mesenchymal cells via activation of FAK and MAPK cascades[3]
Laminin-211
essential for the contractility of airway smooth muscle cells[4][5]
Laminin-121
has a strong affinity for α7β1 integrin, which promotes neurite outgrowth [6]
Laminin-221
Laminin-332
involved in the synthesis of tyrosine, which increase the level of melanin produced by melanocytes[7]
Laminin-311
involved in the maintenance of the alveolar tissue architecture [8]
Laminin-321
Laminin-411
has a vascular role; increases the migration and adhesion of human dermal microvascular endothelial cells (HDMECs), which promote the tubule formation of endothelial cells[9]
Laminin-421
Laminin-511
a potent substrate for up regulating α3β1, which is a promoter for hair growth[10][11]
Laminin-521
essential for the formation of the glomerular filtration barrier (as reviewed in [12]; also involved in preventing Schwann cells from invading the synaptic cleft in a neuromuscular junction [13]
Laminin-213
Laminin-423
Laminin-522
Laminin-523
Laminin 111

Laminin 111 (LM-111) is the one of the first, and predominant, ECM proteins expressed during embryonic development[1][14]. LM-111 provides structural support to the BM[14]. More importantly, this LM isoform’s main role is to regulate muscular regeneration[1][2]. LM-111 is known to prevent the effects of muscular dystrophy, such as skeletal muscle weakness due to damages in cells and tissues[1][2]. It does this by playing a role in myoblast fusion[1], the formation of new and larger myofibres, and acting as a substitute to LM-α2 deficiency[2]. The injection of LM-111 helps re-establish the sarcolemma in muscle cells that are laminin-a2 deficient[2]. This LM isoform also increases muscle integrity by interacting with a7B1 integrin and a-dystroglycan[2], which improves the number of satellite cells by improving satellite cell proliferation[1][2]. LM-111 provides a link between the ECM and the sarcolemma, which prevents muscle degeneration and apoptosis, and promotes muscular adhesion to the basal lamina[2]. There is evidence showing that LM-111 prevents muscle damage. In postexercise mice, those that were treated with the laminin isoform had fewer muscle fibres with centrally located nuclei, which is commonly a sign for muscle damage[1]. LM-111 also plays a role in the epithelial-to-mesenchymal transition (EMT) in cells. A fragment of the LM molecule interacts with matrix metalloproteinases (MMPs), specifically MMP2. The LM-111 fragment down-regulates MMP2, which in turn lowers the amount of BM undergoing degradation[14].

Laminin 211

Laminin 211 (LM-211) plays a role in the contractility of airway smooth muscle (ASM) cells, which relates to the pathology of asthmatic attacks. The expression of this LM isoform in ASM cells is essential for its contractility as well as reducing the levels of proapoptotic proteins in ASM cells [4][5], which results in the hypertrophy of these cells[4]. This relates to asthma because asthmatic airways are characterised to have ASM cells with increased contractility[5]. LM-211 also has a role in the control in the interactions between thymocytes and thymic epithelial cells (TECs). The deposit of LM-211 creates a microenvironment for thymocytes to proliferate, maturate, differentiate, and migrate. Furthermore, the thymocyte-TEC interaction was blocked when antibodies specific for LM-211 were introduced[15].

Laminin 332

Melanocytes are cells that synthesise melanin, a component of the pigmentary system of the skin. The melanin, produced by melanocytes, migrate to keratinocytes for protection. Laminin 332 (LM-332) is derived from keratinocytes and plays a role in the migration and adhesion of melanocytes[7][16]. LM-332 is also promotes the synthesis of melanin in melanocytes by controlling the levels of tyrosine[7]. Tyrosine is essential for the synthesis of melanin and it's level is proportional to the level of melanin i.e. an increase in the level of tyrosine will also increase the level of melanin made[16]. This links to LM-332 because this LM isoform increases the intracellular tyrosine levels and also increases the uptake of extracellular tyrosine[16]. However, the mechanism behind the control of tyrosine levels by LM-322 is still unknown.

Laminin 411

Laminin 411 (LM-411) is expressed in the endothelial BM and plays a significant role in the maintenance of the vascular endothelial BM[9]. Although, Laminin-511 maybe expressed in vascular endothelial BMs as well, LM-411 is expressed in all BMs of all blood vessels, whereas Laminin-511 is only expressed in capillaries and some veins and venules[17]. This LM heterotrimer is involved in the survival of endothelial cells, particularly in their migration and adhesion[9]. The presence of LM-411 increases the migration and adhesion of human dermal microvascular endothelial cells (HDMECs). In turn, the migration of HDMECs promotes tubule formation of endothelial cells[9]. Therefore, it can be deduced that this laminin heterotrimer is involved in vascular formation. Therefore, a lack in LM-411 expression leads to disrupted vascular endothelial BMs. In a study, the lack of LM-411 expression resulted in a bleeding phenotype in newborn mice[17]. LM-411 is related to type IV collage, in that the overexpression of LM-411 increases the number of type IV collagen in capillary BM. The absence of LM-411 leads to no formation of type IV collagen, which affects the assembly of the BM[9].

Laminin 511

Laminin 511 (LM-511) is one of the first ECM proteins expressed during embryogenesis[1]. LM-511 is another LM heterotrimer, release by keratinocytes[18], associated with hair downgrowth[19][18]. Lm-511 is found in the BMZ and interfollicular epithelia but it is most numerous in the BMZ, specifically around the hair follicles[19]. Unlike LMm-332, LM-511 is the primary LM [11] for the stimulation of hair growth and elongation[10]. LM-511 is associated with α3 integrin, in terms of regulating hair growth[19]. α3 integrin acts as a promoter of hair growth[19]. This links back to LM-511, which is a potent substrate for the upregulation the expression of the α3β1 integrin[10][11][18]. Therefore, the presence of LM-511 promotes hair growth via α3β1 integrins[10][11]. Another process as to how LM-511 affects hair follicle involves dermal blood vessels. α3 integrin is also involved in the migration of endothelial cells. Therefore, it is plausible that LM-511 is associated with the recruitment of dermal blood vessels essential for the formation of hair follicles[11]. LM-511 is also involved in the formation of the BMZ. The lack of LM-511 results in a discontinuous lamina densa, which hinders the downgrowth of the hair follicles[18].

Together with LM-411, LM-511 also plays a role in the maintenance of the vascular endothelial BM[17]. Unlike LM-411, LM-511 is expressed only in capillaries and some venules and veins. However, the failure to express LM-411 leads to compensation by LM-511. Due to this event, angiogenesis is increased, which conseuquently enhances the growth of tumours and finally metastasis. Therefore, this LM heterotrimer, even if not directly, is also involed in angiogenesis, tumour formation and metastasis[17].

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 <pubmed>25015639</pubmed>
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 <pubmed>24009313</pubmed>
  3. <pubmed>19895795</pubmed>
  4. 4.0 4.1 4.2 <pubmed>23756649</pubmed>
  5. 5.0 5.1 5.2 <pubmed>19213874</pubmed>
  6. <pubmed>20566382</pubmed>
  7. 7.0 7.1 7.2 <pubmed>24951591</pubmed>
  8. <pubmed>16714422</pubmed>
  9. 9.0 9.1 9.2 9.3 9.4 <pubmed>16374451</pubmed>
  10. 10.0 10.1 10.2 10.3 <pubmed>20211547</pubmed>
  11. 11.0 11.1 11.2 11.3 11.4 <pubmed>12743034</pubmed>
  12. <pubmed>21519194</pubmed>
  13. <pubmed>21766463</pubmed>
  14. 14.0 14.1 14.2 <pubmed>24706882</pubmed>
  15. <pubmed>18644586</pubmed>
  16. 16.0 16.1 16.2 <pubmed>21349841</pubmed>
  17. 17.0 17.1 17.2 17.3 <pubmed>15205311</pubmed>
  18. 18.0 18.1 18.2 18.3 <pubmed>21067603</pubmed>
  19. 19.0 19.1 19.2 19.3 <pubmed>16957169</pubmed>