PMID- 10092817
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20171116
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 162
IP  - 6
DP  - 1999 Mar 15
TI  - C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation
      of phagocytic activity.
PG  - 3583-9
AB  - C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA)
      interact with human monocytes and macrophages, resulting in the enhancement of
      phagocytosis of suboptimally opsonized targets. mAbs that recognize a cell
      surface molecule of 126,000 Mr, designated C1qRP, have been shown to inhibit C1q-
      and MBL-mediated enhancement of phagocytosis. Similar inhibition of the
      SPA-mediated enhancement of phagocytosis by these mAbs now suggests that C1qRP is
      a common component of a receptor for these macromolecules. Ligation of human
      monocytes with immobilized R3, a IgM mAb recognizing C1qRP, also triggers
      enhanced phagocytic capacity of these cells in the absence of ligand, verifying
      the direct involvement of this polypeptide in the regulation of phagocytosis.
      While the cDNA for C1qRP encodes a 631 amino acid membrane protein, Chinese
      hamster ovary cells transfected with the cDNA of the C1qRP coding region express 
      a surface glycoprotein with the identical 126,000 Mr in SDS-PAGE as the native
      C1qRP. Use of glycosylation inhibitors, cleavage of the mature C1qRP with
      specific glycosidases, and in vitro translation of C1qRP cDNA demonstrated that
      both posttranslational glycosylation and the nature of the amino acid sequence of
      the protein contribute to the difference between its predicted m.w. and its
      migration on SDS-PAGE. These results verify that the cDNA cloned codes for the
      mature C1qRP, that C1qRP contains a relatively high degree of O-linked
      glycoslyation, and that C1qRP cross-linked directly by monoclonal anti-C1qRP or
      engaged as a result of cell surface ligation of SPA, as well as C1q and MBL,
      enhances phagocytosis.
FAU - Nepomuceno, R R
AU  - Nepomuceno RR
AD  - Department of Molecular Biology and Biochemistry, University of California,
      Irvine 92697, USA.
FAU - Ruiz, S
AU  - Ruiz S
FAU - Park, M
AU  - Park M
FAU - Tenner, A J
AU  - Tenner AJ
LA  - eng
GR  - AI 41090/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (C1QBP protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (Collectins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Hyaluronan Receptors)
RN  - 0 (Lectins)
RN  - 0 (Mannans)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Proteolipids)
RN  - 0 (Pulmonary Surfactant-Associated Proteins)
RN  - 0 (Pulmonary Surfactants)
RN  - 0 (Receptors, Complement)
RN  - 0 (Recombinant Proteins)
RN  - 0 (complement 1q receptor)
RN  - 80295-33-6 (Complement C1q)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/metabolism/pharmacology
MH  - CHO Cells
MH  - Carrier Proteins/pharmacology
MH  - Collectins
MH  - Complement C1q/*metabolism
MH  - Cricetinae
MH  - DNA, Complementary/metabolism
MH  - Glycosylation
MH  - Humans
MH  - *Hyaluronan Receptors
MH  - Lectins/metabolism
MH  - Mannans/metabolism
MH  - Membrane Glycoproteins/antagonists & inhibitors/genetics/metabolism/*physiology
MH  - Mitochondrial Proteins
MH  - Molecular Mimicry
MH  - Phagocytosis/*immunology
MH  - Protein Biosynthesis/immunology
MH  - Proteolipids/antagonists & inhibitors/pharmacology
MH  - Pulmonary Surfactant-Associated Proteins
MH  - Pulmonary Surfactants/antagonists & inhibitors/pharmacology
MH  - Receptors, Complement/antagonists & inhibitors/genetics/metabolism/*physiology
MH  - Recombinant Proteins/biosynthesis
MH  - U937 Cells
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1999 Mar 15;162(6):3583-9.