PMID- 7543245
OWN - NLM
STAT- MEDLINE
DCOM- 19950901
LR  - 20171213
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 269
IP  - 1 Pt 1
DP  - 1995 Jul
TI  - MCP-1-stimulated monocytes preferentially utilize beta 2-integrins to migrate on 
      laminin and fibronectin.
PG  - C60-8
AB  - Recruitment of monocytes to inflammatory sites involves a series of sequential 
      attachments and detachments to extracellular matrix proteins in response to a 
      chemoattractant gradient. In this study we compared the migration of human 
      peripheral blood monocytes on different extracellular matrix proteins in response 
      to monocyte chemoattractant protein-1 (MCP-1) and 
      N-formylmethionyl-leucyl-phenylalanine. Monocytes migrated more effectively on 
      laminin compared with other extracellular matrix proteins. In contrast, this 
      preference was not observed with neutrophils, suggesting that the monocytes and 
      neutrophils may have differences in their migration on extracellular matrix 
      proteins. To study this further, function-blocking monoclonal antibodies were 
      used to examine mechanistically whether beta 1- and beta 2-integrins were 
      involved in monocyte migration on fibronectin or laminin in response to MCP-1. 
      Monocyte migration on both laminin and fibronectin was blocked 100% (P < 0.05) by 
      intact monoclonal antibody, F(ab') fragments, and F(ab')2 fragments to beta 
      2-integrins. We also determined that antibodies to beta 2-integrins block 
      monocyte migration that has already been initiated. In contrast, antibody to the 
      beta 1-integrins inhibited monocyte migration by approximately 40% (P < 0.05). 
      Thus monocytes that express both beta 1- and beta 2-integrins require utilization 
      of beta 2-integrins in migration on extracellular matrix proteins. The results 
      also suggest that beta 1-integrins facilitate monocyte migration but that 
      monocyte migration is not absolutely dependent on the interaction of beta 
      1-integrins with extracellular matrix proteins. In contrast, neutrophil migration 
      is beta 2-integrin dependent and is not facilitated by beta 1-integrins.
FAU - Penberthy, T W
AU  - Penberthy TW
AD  - Division of Oral Biology, Boston University School of Graduate Dentistry, 
      Massachusetts 02118, USA.
FAU - Jiang, Y
AU  - Jiang Y
FAU - Luscinskas, F W
AU  - Luscinskas FW
FAU - Graves, D T
AU  - Graves DT
LA  - eng
GR  - DE-07559/DE/NIDCR NIH HHS/United States
GR  - HL-36028/HL/NHLBI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - 0 (CD18 Antigens)
RN  - 0 (Chemokine CCL2)
RN  - 0 (Chemotactic Factors)
RN  - 0 (Cytokines)
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Fibronectins)
RN  - 0 (Integrin beta1)
RN  - 0 (Integrins)
RN  - 0 (Laminin)
RN  - 9012-36-6 (Sepharose)
SB  - IM
MH  - CD18 Antigens
MH  - Cell Movement/physiology
MH  - Chemokine CCL2
MH  - Chemotactic Factors/*pharmacology
MH  - Cytokines/pharmacology
MH  - Extracellular Matrix Proteins
MH  - *Fibronectins
MH  - Humans
MH  - Integrin beta1
MH  - Integrins/*physiology
MH  - *Laminin
MH  - Monocytes/*drug effects/*physiology
MH  - Sepharose
EDAT- 1995/07/01 00:00
MHDA- 1995/07/01 00:01
CRDT- 1995/07/01 00:00
PHST- 1995/07/01 00:00 [pubmed]
PHST- 1995/07/01 00:01 [medline]
PHST- 1995/07/01 00:00 [entrez]
AID - 10.1152/ajpcell.1995.269.1.C60 [doi]
PST - ppublish
SO  - Am J Physiol. 1995 Jul;269(1 Pt 1):C60-8. doi: 10.1152/ajpcell.1995.269.1.C60.