PMID- 7686157
OWN - NLM
STAT- MEDLINE
DCOM- 19930727
LR  - 20231213
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 268
IP  - 19
DP  - 1993 Jul 5
TI  - Molecular cloning and characterization of ficolin, a multimeric protein with 
      fibrinogen- and collagen-like domains.
PG  - 14505-13
AB  - We have previously identified and purified transforming growth factor-beta 1 
      (TGF-beta 1)-binding proteins from porcine uterus membranes (Ichijo, H., 
      Ronnstrand, L., Miyagawa, K., Ohashi, H., Heldin, C.-H., and Miyazono, K. (1991) 
      J. Biol. Chem. 266, 22459-22464). One of these TGF-beta 1-binding proteins, with 
      a molecular weight of 40,000, was purified to homogeneity and subjected to amino 
      acid sequence analysis. The amino acid sequences obtained were used to isolate 
      two closely related cDNA clones from a porcine uterus cDNA library. The deduced 
      amino acid sequences revealed that both cDNAs encoded proteins that were mainly 
      composed of fibrinogen-like and collagen-like domains. Therefore, they were 
      denoted ficolin-alpha and ficolin-beta. Expression of ficolin-alpha and -beta 
      cDNA in mammalian cells revealed that ficolin forms dimers, trimers, and several 
      higher order of oligomers, whose molecular weights fit well with those of the 
      purified TGF-beta 1-binding proteins from porcine uterus. Moreover, 
      immunoblotting analysis using a peptide anti-serum against ficolin indicated that 
      the TGF-beta 1-binding proteins identified in porcine uterus are ficolin-alpha, 
      -beta, and their oligomers or closely related molecules. However, recombinant 
      ficolin-alpha and -beta did not bind TGF-beta 1, despite the similarities in 
      molecular weights and immunoreactivity with the material from the natural source. 
      It is possible that a specific posttranslational modification of ficolin or 
      interaction with another component is needed for TGF-beta 1 binding. Analysis by 
      Northern blotting revealed that the expression of ficolin-alpha mRNA is 
      relatively restricted and most abundant in placenta and lung. On the other hand, 
      ficolin-beta was mainly expressed in skeletal muscle. The in vivo functions of 
      ficolin will be discussed.
FAU - Ichijo, H
AU  - Ichijo H
AD  - Ludwig Institute for Cancer Research, Uppsala, Sweden.
FAU - Hellman, U
AU  - Hellman U
FAU - Wernstedt, C
AU  - Wernstedt C
FAU - Gonez, L J
AU  - Gonez LJ
FAU - Claesson-Welsh, L
AU  - Claesson-Welsh L
FAU - Heldin, C H
AU  - Heldin CH
FAU - Miyazono, K
AU  - Miyazono K
LA  - eng
SI  - GENBANK/L12344
SI  - GENBANK/L12345
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Lectins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Peptide Fragments)
RN  - 0 (RNA, Messenger)
RN  - 0 (Transforming Growth Factor beta)
RN  - 24937-83-5 (Poly A)
RN  - 63231-63-0 (RNA)
RN  - 9001-32-5 (Fibrinogen)
RN  - 9007-34-5 (Collagen)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Carrier Proteins/biosynthesis/*genetics/isolation & purification
MH  - Chromatography, Affinity
MH  - Cloning, Molecular/methods
MH  - Collagen/*genetics
MH  - DNA
MH  - Female
MH  - Fibrinogen/*genetics
MH  - Gene Expression
MH  - Gene Library
MH  - Humans
MH  - *Lectins
MH  - Macromolecular Substances
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Peptide Fragments/isolation & purification
MH  - Poly A/genetics/isolation & purification
MH  - RNA/genetics/isolation & purification
MH  - RNA, Messenger
MH  - Sequence Homology, Amino Acid
MH  - Swine
MH  - Transfection
MH  - Transforming Growth Factor beta/metabolism
MH  - Uterus/*metabolism
MH  - Ficolins
EDAT- 1993/07/05 00:00
MHDA- 1993/07/05 00:01
CRDT- 1993/07/05 00:00
PHST- 1993/07/05 00:00 [pubmed]
PHST- 1993/07/05 00:01 [medline]
PHST- 1993/07/05 00:00 [entrez]
AID - S0021-9258(19)85267-5 [pii]
PST - ppublish
SO  - J Biol Chem. 1993 Jul 5;268(19):14505-13.