Abstract
Hyaluronan is a constituent of the extracellular matrix of connective tissue and is actively synthesized during wound healing and tissue repair to provide a frame-work for ingrowth of blood vessels and fibroblasts. Changes in the serum concentration of hyaluronan are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis. In addition, hyaluronan has been implicated as an important substrate for migration of adhesion of leukocytes during inflammation. A human hyaluronan synthase (HuHAS1) cDNA was isolated by a functional expression cloning approach. Transfection of CHO cells conferred hyaluronidase-sensitive adhesiveness of a mucosal T cell line via the lymphocyte hyaluronan receptor, CD44, as well as increased hyaluronan levels in the cultures of transfected cells. The HuHAS1 amino acid sequence shows considerable homology to the hasA gene product of Streptococcus pyogenes, a glycosaminoglycan synthetase from Xenopus laevis (DG42), and is the human homolog of a recently described murine hyaluronan synthase.
| Original language | English |
|---|---|
| Pages (from-to) | 23395-23399 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 271 |
| Issue number | 38 |
| DOIs | |
| Publication status | Published - 1996 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Functional cloning of the cDNA for a human hyaluronan synthase. / Shyjan, Anne M.; Heldin, Paraskevi; Butcher, Eugene C.; Yoshino, Tadashi; Briskin, Michael J.
In: Journal of Biological Chemistry, Vol. 271, No. 38, 1996, p. 23395-23399.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Functional cloning of the cDNA for a human hyaluronan synthase
AU - Shyjan, Anne M.
AU - Heldin, Paraskevi
AU - Butcher, Eugene C.
AU - Yoshino, Tadashi
AU - Briskin, Michael J.
PY - 1996
Y1 - 1996
N2 - Hyaluronan is a constituent of the extracellular matrix of connective tissue and is actively synthesized during wound healing and tissue repair to provide a frame-work for ingrowth of blood vessels and fibroblasts. Changes in the serum concentration of hyaluronan are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis. In addition, hyaluronan has been implicated as an important substrate for migration of adhesion of leukocytes during inflammation. A human hyaluronan synthase (HuHAS1) cDNA was isolated by a functional expression cloning approach. Transfection of CHO cells conferred hyaluronidase-sensitive adhesiveness of a mucosal T cell line via the lymphocyte hyaluronan receptor, CD44, as well as increased hyaluronan levels in the cultures of transfected cells. The HuHAS1 amino acid sequence shows considerable homology to the hasA gene product of Streptococcus pyogenes, a glycosaminoglycan synthetase from Xenopus laevis (DG42), and is the human homolog of a recently described murine hyaluronan synthase.
AB - Hyaluronan is a constituent of the extracellular matrix of connective tissue and is actively synthesized during wound healing and tissue repair to provide a frame-work for ingrowth of blood vessels and fibroblasts. Changes in the serum concentration of hyaluronan are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis. In addition, hyaluronan has been implicated as an important substrate for migration of adhesion of leukocytes during inflammation. A human hyaluronan synthase (HuHAS1) cDNA was isolated by a functional expression cloning approach. Transfection of CHO cells conferred hyaluronidase-sensitive adhesiveness of a mucosal T cell line via the lymphocyte hyaluronan receptor, CD44, as well as increased hyaluronan levels in the cultures of transfected cells. The HuHAS1 amino acid sequence shows considerable homology to the hasA gene product of Streptococcus pyogenes, a glycosaminoglycan synthetase from Xenopus laevis (DG42), and is the human homolog of a recently described murine hyaluronan synthase.
UR - http://www.scopus.com/inward/record.url?scp=0029817363&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029817363&partnerID=8YFLogxK
U2 - 10.1074/jbc.271.38.23395
DO - 10.1074/jbc.271.38.23395
M3 - Article
C2 - 8798544
AN - SCOPUS:0029817363
VL - 271
SP - 23395
EP - 23399
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 38
ER -