Collagen- and collagen peptide-induced chemotaxis of human blood monocytes*

Research output: Contribution to journalArticle

148 Citations (Scopus)

Abstract

The ability of collagen and collagen-derived peptides to act as chemotactic stimuli was investigated by in vitro chemotaxis assays. Native human and chick skin collagen (type I) and α-chains obtained from purified chick skin collagen were each chemotactic for human peripheral blood monocytes. In addition, smaller peptides obtained either by digesting native collagen with bacterial collagenase or by degrading purified α-chains with cyanogen bromide or pepsin were also chemotactic for monocytes. In contrast, native collagen, α-chains, and smaller collagen-derived peptides were not chemotactic for human neutrophils. Since collagen is degraded at sites of tissue damage and inflammation, our findings suggest the possibility that such collagen-derived degradation products might directly serve as chemotactic stimuli for human peripheral blood monocytes in vivo.

Original languageEnglish (US)
Pages (from-to)1299-1307
Number of pages9
JournalJournal of Experimental Medicine
Volume143
Issue number6
DOIs
StatePublished - Jun 1 1976

Fingerprint

Chemotaxis
Monocytes
Collagen
Peptides
Cyanogen Bromide
Skin
Aptitude
Pepsin A
Collagenases
Collagen Type I
Population Groups
Neutrophils
Inflammation

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

Cite this

Collagen- and collagen peptide-induced chemotaxis of human blood monocytes*. / Postlethwaite, Arnold; Kang, Andrew.

In: Journal of Experimental Medicine, Vol. 143, No. 6, 01.06.1976, p. 1299-1307.

Research output: Contribution to journalArticle

@article{74f674dcd7614d03a30ffceb83d9758b,
title = "Collagen- and collagen peptide-induced chemotaxis of human blood monocytes*",
abstract = "The ability of collagen and collagen-derived peptides to act as chemotactic stimuli was investigated by in vitro chemotaxis assays. Native human and chick skin collagen (type I) and α-chains obtained from purified chick skin collagen were each chemotactic for human peripheral blood monocytes. In addition, smaller peptides obtained either by digesting native collagen with bacterial collagenase or by degrading purified α-chains with cyanogen bromide or pepsin were also chemotactic for monocytes. In contrast, native collagen, α-chains, and smaller collagen-derived peptides were not chemotactic for human neutrophils. Since collagen is degraded at sites of tissue damage and inflammation, our findings suggest the possibility that such collagen-derived degradation products might directly serve as chemotactic stimuli for human peripheral blood monocytes in vivo.",
author = "Arnold Postlethwaite and Andrew Kang",
year = "1976",
month = "6",
day = "1",
doi = "10.1084/jem.143.6.1299",
language = "English (US)",
volume = "143",
pages = "1299--1307",
journal = "Journal of Experimental Medicine",
issn = "0022-1007",
publisher = "Rockefeller University Press",
number = "6",

}

TY - JOUR

T1 - Collagen- and collagen peptide-induced chemotaxis of human blood monocytes*

AU - Postlethwaite, Arnold

AU - Kang, Andrew

PY - 1976/6/1

Y1 - 1976/6/1

N2 - The ability of collagen and collagen-derived peptides to act as chemotactic stimuli was investigated by in vitro chemotaxis assays. Native human and chick skin collagen (type I) and α-chains obtained from purified chick skin collagen were each chemotactic for human peripheral blood monocytes. In addition, smaller peptides obtained either by digesting native collagen with bacterial collagenase or by degrading purified α-chains with cyanogen bromide or pepsin were also chemotactic for monocytes. In contrast, native collagen, α-chains, and smaller collagen-derived peptides were not chemotactic for human neutrophils. Since collagen is degraded at sites of tissue damage and inflammation, our findings suggest the possibility that such collagen-derived degradation products might directly serve as chemotactic stimuli for human peripheral blood monocytes in vivo.

AB - The ability of collagen and collagen-derived peptides to act as chemotactic stimuli was investigated by in vitro chemotaxis assays. Native human and chick skin collagen (type I) and α-chains obtained from purified chick skin collagen were each chemotactic for human peripheral blood monocytes. In addition, smaller peptides obtained either by digesting native collagen with bacterial collagenase or by degrading purified α-chains with cyanogen bromide or pepsin were also chemotactic for monocytes. In contrast, native collagen, α-chains, and smaller collagen-derived peptides were not chemotactic for human neutrophils. Since collagen is degraded at sites of tissue damage and inflammation, our findings suggest the possibility that such collagen-derived degradation products might directly serve as chemotactic stimuli for human peripheral blood monocytes in vivo.

UR - http://www.scopus.com/inward/record.url?scp=85012405294&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85012405294&partnerID=8YFLogxK

U2 - 10.1084/jem.143.6.1299

DO - 10.1084/jem.143.6.1299

M3 - Article

VL - 143

SP - 1299

EP - 1307

JO - Journal of Experimental Medicine

JF - Journal of Experimental Medicine

SN - 0022-1007

IS - 6

ER -