Reconstruction of basement membrane in skin equivalent; role of laminin-1
To reconstruct the basement membrane in a skin equivalent, the epidermodermal interface was coated with porcine type IV collagen and mouse laminin-1 at various ratios before keratinocyte seeding. Laminin-1, a component of the basement membrane, induced massive infiltration of keratinocytes into the...
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Veröffentlicht in: | Archives of Dermatological Research 2001-07, Vol.293 (7), p.356-362 |
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creator | JAE YOUN YI YONG HA YOON YOUNG SOOK SON HYUN SOOK PARK CHUN HO KIM CHANG HWAN KIM HYUN JOO KANG LEE, Eunah YOUN YOUNG KIM YONG JAE JIN TAE HWAN KIM |
description | To reconstruct the basement membrane in a skin equivalent, the epidermodermal interface was coated with porcine type IV collagen and mouse laminin-1 at various ratios before keratinocyte seeding. Laminin-1, a component of the basement membrane, induced massive infiltration of keratinocytes into the dermal equivalent, while type IV collagen induced discrete demarcation between dermal and epidermal compartments without any infiltrating cells. Immunohistochemical staining indicated that the laminin-induced infiltrating cells expressed endogenous type IV collagens at the cell periphery, which were not incorporated into the basement membrane structure. The infiltrating cells did not express fibronectin receptor alpha5beta1 integrin but showed MMP-9 secretion and cell surface associated MMP-2. However, when laminin-1 was preincubated with type IV collagen, laminin-1-induced keratinocyte infiltration as well as MMP-9 induction were almost completely suppressed to basal levels. Therefore, replenishment of the type IV collagen lattice seemed to cause laminin-stimulated cells to anchor to the lattice, in a similar manner to the basal cells on the basement membrane of normal skin. Our study suggests that the molar ratio of basement membrane components may determine the behavior of basal cells within the wound healing microenvironment, which is probably regulated either by extracellular matrix deposition or degradation. |
doi_str_mv | 10.1007/s004030100234 |
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Laminin-1, a component of the basement membrane, induced massive infiltration of keratinocytes into the dermal equivalent, while type IV collagen induced discrete demarcation between dermal and epidermal compartments without any infiltrating cells. Immunohistochemical staining indicated that the laminin-induced infiltrating cells expressed endogenous type IV collagens at the cell periphery, which were not incorporated into the basement membrane structure. The infiltrating cells did not express fibronectin receptor alpha5beta1 integrin but showed MMP-9 secretion and cell surface associated MMP-2. However, when laminin-1 was preincubated with type IV collagen, laminin-1-induced keratinocyte infiltration as well as MMP-9 induction were almost completely suppressed to basal levels. Therefore, replenishment of the type IV collagen lattice seemed to cause laminin-stimulated cells to anchor to the lattice, in a similar manner to the basal cells on the basement membrane of normal skin. Our study suggests that the molar ratio of basement membrane components may determine the behavior of basal cells within the wound healing microenvironment, which is probably regulated either by extracellular matrix deposition or degradation.</description><identifier>ISSN: 0340-3696</identifier><identifier>EISSN: 1432-069X</identifier><identifier>DOI: 10.1007/s004030100234</identifier><identifier>PMID: 11550809</identifier><identifier>CODEN: ADREDL</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>3T3 Cells ; Animals ; Antigens, Surface - physiology ; Basal cells ; Basement Membrane - physiology ; Basement membranes ; Biological and medical sciences ; Cell surface ; Collagen ; Collagen (type IV) ; Collagen Type IV - physiology ; Dermatology ; Extracellular matrix ; Fibronectin ; Fibronectins - pharmacology ; Gelatinase A ; Gelatinase B ; Integrin alpha6beta4 ; Integrins - physiology ; Keratinocytes ; Keratinocytes - drug effects ; Keratinocytes - physiology ; Laminin ; Laminin - antagonists & inhibitors ; Laminin - physiology ; Matrix Metalloproteinase 2 - physiology ; Matrix Metalloproteinase 9 - physiology ; Medical sciences ; Membrane structure ; Mice ; Skin ; Skin involvement in other diseases. Miscellaneous. General aspects ; Skin, Artificial ; Swine ; Wound healing</subject><ispartof>Archives of Dermatological Research, 2001-07, Vol.293 (7), p.356-362</ispartof><rights>2001 INIST-CNRS</rights><rights>Archives of Dermatological Research is a copyright of Springer, (2001). 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Laminin-1, a component of the basement membrane, induced massive infiltration of keratinocytes into the dermal equivalent, while type IV collagen induced discrete demarcation between dermal and epidermal compartments without any infiltrating cells. Immunohistochemical staining indicated that the laminin-induced infiltrating cells expressed endogenous type IV collagens at the cell periphery, which were not incorporated into the basement membrane structure. The infiltrating cells did not express fibronectin receptor alpha5beta1 integrin but showed MMP-9 secretion and cell surface associated MMP-2. However, when laminin-1 was preincubated with type IV collagen, laminin-1-induced keratinocyte infiltration as well as MMP-9 induction were almost completely suppressed to basal levels. Therefore, replenishment of the type IV collagen lattice seemed to cause laminin-stimulated cells to anchor to the lattice, in a similar manner to the basal cells on the basement membrane of normal skin. Our study suggests that the molar ratio of basement membrane components may determine the behavior of basal cells within the wound healing microenvironment, which is probably regulated either by extracellular matrix deposition or degradation.</description><subject>3T3 Cells</subject><subject>Animals</subject><subject>Antigens, Surface - physiology</subject><subject>Basal cells</subject><subject>Basement Membrane - physiology</subject><subject>Basement membranes</subject><subject>Biological and medical sciences</subject><subject>Cell surface</subject><subject>Collagen</subject><subject>Collagen (type IV)</subject><subject>Collagen Type IV - physiology</subject><subject>Dermatology</subject><subject>Extracellular matrix</subject><subject>Fibronectin</subject><subject>Fibronectins - pharmacology</subject><subject>Gelatinase A</subject><subject>Gelatinase B</subject><subject>Integrin alpha6beta4</subject><subject>Integrins - physiology</subject><subject>Keratinocytes</subject><subject>Keratinocytes - drug effects</subject><subject>Keratinocytes - physiology</subject><subject>Laminin</subject><subject>Laminin - antagonists & inhibitors</subject><subject>Laminin - physiology</subject><subject>Matrix Metalloproteinase 2 - physiology</subject><subject>Matrix Metalloproteinase 9 - physiology</subject><subject>Medical sciences</subject><subject>Membrane structure</subject><subject>Mice</subject><subject>Skin</subject><subject>Skin involvement in other diseases. 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Laminin-1, a component of the basement membrane, induced massive infiltration of keratinocytes into the dermal equivalent, while type IV collagen induced discrete demarcation between dermal and epidermal compartments without any infiltrating cells. Immunohistochemical staining indicated that the laminin-induced infiltrating cells expressed endogenous type IV collagens at the cell periphery, which were not incorporated into the basement membrane structure. The infiltrating cells did not express fibronectin receptor alpha5beta1 integrin but showed MMP-9 secretion and cell surface associated MMP-2. However, when laminin-1 was preincubated with type IV collagen, laminin-1-induced keratinocyte infiltration as well as MMP-9 induction were almost completely suppressed to basal levels. Therefore, replenishment of the type IV collagen lattice seemed to cause laminin-stimulated cells to anchor to the lattice, in a similar manner to the basal cells on the basement membrane of normal skin. Our study suggests that the molar ratio of basement membrane components may determine the behavior of basal cells within the wound healing microenvironment, which is probably regulated either by extracellular matrix deposition or degradation.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>11550809</pmid><doi>10.1007/s004030100234</doi><tpages>7</tpages></addata></record> |
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subjects | 3T3 Cells Animals Antigens, Surface - physiology Basal cells Basement Membrane - physiology Basement membranes Biological and medical sciences Cell surface Collagen Collagen (type IV) Collagen Type IV - physiology Dermatology Extracellular matrix Fibronectin Fibronectins - pharmacology Gelatinase A Gelatinase B Integrin alpha6beta4 Integrins - physiology Keratinocytes Keratinocytes - drug effects Keratinocytes - physiology Laminin Laminin - antagonists & inhibitors Laminin - physiology Matrix Metalloproteinase 2 - physiology Matrix Metalloproteinase 9 - physiology Medical sciences Membrane structure Mice Skin Skin involvement in other diseases. Miscellaneous. General aspects Skin, Artificial Swine Wound healing |
title | Reconstruction of basement membrane in skin equivalent; role of laminin-1 |
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