Differences between scar and dermal cultured fibroblasts derived from a patient with recurrent abdominal incision wound herniation.
Fibroblasts were derived from dermis and scar of a 47-year-old white man with a recurrent incisional hernia as a result of fractured ribs. The scar was thin and stretched, suggesting a defect in the maturation of granulation tissue. After surgical repair, biopsy specimens of discarded scar and skin were used to generate fibroblast cell lines. Fibroblasts maintained in medium containing 10% fetal bovine serum and antibiotic were studied between their third and eighth passage. By phase contrast microscopy, no structural differences were obvious, but it was noted that to pass scar fibroblasts, a more aggressive trypsin regimen was required. Immunohistologic and Western blot analysis of patient scar fibroblasts showed (1) more a smooth muscle actin within stress fibers, (2) increased expression of the vitronectin integrin receptor alpha(v) (CD 51), and (3) reduced expression of the collagen integrin receptor alpha2 (CD 49b). The expression of vinculin from focal adhesions or a tubulin from microtubules was the same among cell lines. Contractions of scar and dermal fibroblast-populated collagen lattice were compared. At 24 hours, contractions were 69 percent with newborn fibroblasts (normal); 68 percent for patient dermal fibroblasts; and only 48 percent for patient scar fibroblasts. The retarded contraction of scar fibroblast-populated collagen lattice was significant (p > or = 0.002). Myosin ATPase activity, critical for lattice contraction, and cell migration were equivalent among all cell lines. A plausible mechanism for the retardation of scar lattice contraction is disruption of fibroblasts and collagen interactions, for which the attachment of cells to collagen is altered. It is proposed that either the decrease in the expression of collagen integrin receptor alpha2 (CD 49b), an increase in the expression of the vitronectin receptor alpha(v) (CD 51), or a combination of both is responsible for disruption of collagen fibroblast interactions.
Boemi
L
L
Department of Surgery, Milton S. Hershey Medical Center, Pennsylvania State University College of Medicine, Hershey, USA.
Allison
G M
GM
Graham
W P
WP
Krummel
T M
TM
Ehrlich
H P
HP
D000199:Actins / Q000032:analysis; D015703:Antigens, CD / Q000378:metabolism; D015153:Blotting, Western; D002465:Cell Movement; D002478:Cells, Cultured; D002921:Cicatrix / Q000209:etiology / Q000473:pathology* / Q000503:physiopathology; D003094:Collagen / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism* / Q000473:pathology / Q000502:physiology; D059685:Herniorrhaphy; D006801:Humans; D007150:Immunohistochemistry; D039421:Integrin alpha2; D039564:Integrin alphaV; D007813:Laparotomy / Q000009:adverse effects*; D008297:Male; D008875:Middle Aged; D009218:Myosins / Q000378:metabolism; D012008:Recurrence; D012086:Reoperation; D012867:Skin / Q000473:pathology*; D016596:Vinculin / Q000378:metabolism; D014945:Wound Healing
D000199:Actins; D015703:Antigens, CD; D039421:Integrin alpha2; D039564:Integrin alphaV; D016596:Vinculin; D003094:Collagen; D009218:Myosins