TY - JOUR
T1 - Differential distribution of five members of the matrix metalloproteinase family and one inhibitor (TIMP-1) in human liver and skin
AU - Geisler, S.
AU - Lichtinghagen, R.
AU - Böker, K. H.W.
AU - Veh, R. W.
PY - 1997/7/16
Y1 - 1997/7/16
N2 - Matrix metalloproteinases represent a family of zinc-dependent proteolytic enzymes thought to be involved in normal and disease-related tissue remodeling processes. Increasing information about these enzymes is becoming available concerning their primary sequences, regulation at the mRNA level, activation of proenzymes, and modulation of enzyme activity by tissue inhibitors. In contrast, their morphological distribution and biological functions in normal tissues are poorly understood. In the present report, the comparative distribution of five members (gelatinase-A, gelatinase-B, matrilysin, stromelysin-l, and stromelysin-3) of the matrix metalloproteinase family and of one inhibitor (TIMP-1) has been morphologically analyzed in human liver and skin with the aid of new monospecific antibodies. Because of their common designation as matrix proteinases, these enzymes might have been expected to be distributed throughout these tissues, or at least in the connective tissue. However, each member of the family produces a highly specific pattern, staining structures such as arteriolar smooth muscle cells, myoepithelial cells in secretory portions or the luminal lining in excretory ducts of dermal sweat glands, liver bile canaliculi, or structures surrounding peripheral nerve axons. No reactivity is detected in rat tissues.
AB - Matrix metalloproteinases represent a family of zinc-dependent proteolytic enzymes thought to be involved in normal and disease-related tissue remodeling processes. Increasing information about these enzymes is becoming available concerning their primary sequences, regulation at the mRNA level, activation of proenzymes, and modulation of enzyme activity by tissue inhibitors. In contrast, their morphological distribution and biological functions in normal tissues are poorly understood. In the present report, the comparative distribution of five members (gelatinase-A, gelatinase-B, matrilysin, stromelysin-l, and stromelysin-3) of the matrix metalloproteinase family and of one inhibitor (TIMP-1) has been morphologically analyzed in human liver and skin with the aid of new monospecific antibodies. Because of their common designation as matrix proteinases, these enzymes might have been expected to be distributed throughout these tissues, or at least in the connective tissue. However, each member of the family produces a highly specific pattern, staining structures such as arteriolar smooth muscle cells, myoepithelial cells in secretory portions or the luminal lining in excretory ducts of dermal sweat glands, liver bile canaliculi, or structures surrounding peripheral nerve axons. No reactivity is detected in rat tissues.
KW - Collagen
KW - Fat-storing cells
KW - Fibrocytes
KW - Human
KW - Matrilysin (PUMP)
KW - Peripheral nerve glial cells
KW - Tumors
KW - Wound healing
UR - http://www.scopus.com/inward/record.url?scp=0031011325&partnerID=8YFLogxK
U2 - 10.1007/s004410050863
DO - 10.1007/s004410050863
M3 - Article
C2 - 9182612
AN - SCOPUS:0031011325
VL - 289
SP - 173
EP - 183
JO - Cell and Tissue Research
JF - Cell and Tissue Research
SN - 0302-766X
IS - 1
ER -