PMID- 3005361
OWN - NLM
STAT- MEDLINE
DCOM- 19860424
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 77
IP  - 3
DP  - 1986 Mar
TI  - Effects of fibrinogen derivatives upon the inflammatory response. Studies with 
      human fibrinopeptide B.
PG  - 1014-9
AB  - Fibrin formation and turnover are intimately associated with inflammation and 
      wound healing. To explore whether fibrin(ogen)-derived peptides exert direct 
      effects upon cells involved in inflammation and tissue repair we examined the 
      capacity of human fibrinopeptide B (hFpB), a thrombin-derived proteolytic 
      cleavage product of the fibrinogen B beta-chain, to stimulate neutrophils (PMN), 
      monocytes, and fibroblasts. hFpB caused directed cell migration of PMN and 
      fibroblasts that was optimal at approximately 10(-8) M. This chemotactic activity 
      was blocked by preincubating hFpB with antiserum to hFpB. hFpB was not 
      chemotactic for monocytes. The chemotactic potency of hFpB for PMN was equivalent 
      to that of anaphylatoxin from the fifth component of human complement (C5a), 
      leukotriene B4 (LTB4), and formyl-methionyl-leucyl-phenylalanine (fMLP), and for 
      fibroblasts its chemotactic activity was comparable to that of platelet-derived 
      growth factor. hFpB did not interact with PMN receptors for C5a, LTB4, or fMLP as 
      (a) desensitization with 10(-7) M hFpB abolished chemotaxis to hFpB but had no 
      effect upon chemotaxis to C5a, LTB4, or fMLP and (b) induction of chemotactic 
      responses to fMLP and LTB4 in neutrophilic leukemic cells (HL-60 cells) by 
      incubation with dimethylsulfoxide did not extend to hFpB. Like fMLP, hFpB caused 
      a rapid, dose-dependent increase in PMN cytoskeletal associated actin, but unlike 
      fMLP, hFpB did not cause PMN aggregation, release of lysosomal enzymes (lysozyme 
      and beta-glucuronidase), or the production of superoxide anion. These results 
      suggest that hFpB may have a role in recruiting PMN and fibroblasts at sites of 
      fibrin deposition and turnover. The capacity of hFpB to cause PMN chemotaxis 
      without causing concurrent release of lysosomal enzymes or the production of 
      superoxide anion is further evidence for the complexity of PMN responses to 
      chemotactic agents.
FAU - Senior, R M
AU  - Senior RM
FAU - Skogen, W F
AU  - Skogen WF
FAU - Griffin, G L
AU  - Griffin GL
FAU - Wilner, G D
AU  - Wilner GD
LA  - eng
GR  - 2T32 HL07038/HL/NHLBI NIH HHS/United States
GR  - HL14147/HL/NHLBI NIH HHS/United States
GR  - HL29594/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Actins)
RN  - 0 (Complement C5)
RN  - 11062-77-4 (Superoxides)
RN  - 1HGW4DR56D (Leukotriene B4)
RN  - 25422-31-5 (Fibrinopeptide A)
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
RN  - 80295-54-1 (Complement C5a)
RN  - 9001-32-5 (Fibrinogen)
RN  - EC 3.2.1.31 (Glucuronidase)
RN  - YOW8V9698H (Dimethyl Sulfoxide)
SB  - IM
MH  - Actins/physiology
MH  - Cell Aggregation
MH  - Cell Membrane/metabolism
MH  - Cells, Cultured
MH  - *Chemotaxis, Leukocyte
MH  - Complement C5/physiology
MH  - Complement C5a
MH  - Dimethyl Sulfoxide/pharmacology
MH  - Fibrinogen/*physiology
MH  - Fibrinopeptide A/*physiology
MH  - Fibroblasts/physiology
MH  - Glucuronidase/metabolism
MH  - Humans
MH  - Inflammation/*physiopathology
MH  - Leukotriene B4/physiology
MH  - Lysosomes/enzymology
MH  - N-Formylmethionine Leucyl-Phenylalanine/physiology
MH  - Neutrophils/*physiology/ultrastructure
MH  - Superoxides/metabolism
PMC - PMC423507
EDAT- 1986/03/01 00:00
MHDA- 1986/03/01 00:01
PMCR- 1986/03/01
CRDT- 1986/03/01 00:00
PHST- 1986/03/01 00:00 [pubmed]
PHST- 1986/03/01 00:01 [medline]
PHST- 1986/03/01 00:00 [entrez]
PHST- 1986/03/01 00:00 [pmc-release]
AID - 10.1172/JCI112353 [doi]
PST - ppublish
SO  - J Clin Invest. 1986 Mar;77(3):1014-9. doi: 10.1172/JCI112353.