PMID- 10611155
OWN - NLM
STAT- MEDLINE
DCOM- 20000119
LR  - 20190707
IS  - 0016-5085 (Print)
IS  - 0016-5085 (Linking)
VI  - 118
IP  - 1
DP  - 2000 Jan
TI  - pS2/TFF1 interacts directly with the VWFC cysteine-rich domains of mucins.
PG  - 70-80
AB  - BACKGROUND & AIMS: Trefoil factors (TFFs) are secreted gastrointestinal proteins 
      that have been shown to protect and promote healing of the gastrointestinal
      tract. Moreover, pS2/TFF1 is essential for normal differentiation of the gastric 
      mucosa because deficient mice develop antropyloric adenomas. To date, it is
      unclear how TFFs mediate their functions. METHODS: Using the yeast 2-hybrid
      system, we attempted to identify murine TFF1 interacting proteins by screening a 
      stomach and duodenum complementary DNA (cDNA) expression library. RESULTS: Four
      positive clones were isolated. Sequence and expression studies showed that they
      corresponded to the murine counterpart of human cDNA sequences encoding
      carboxy-terminal fragments of mMuc2 (489 residues) and mMuc5AC (427, 430, and 894
      residues) mucin proteins. Mutagenesis experiments showed that TFF1 interacts with
      the 2 mucins through binding with their VWFC1 and VWFC2 (von Willebrand factor C)
      cysteine-rich domains. CONCLUSIONS: These results show that the gastrointestinal 
      protective effect of TFF1, and presumably of the other TFFs, is caused at least
      partially by their participation, via mucin binding, in the correct organization 
      of the mucous layer that protects the apical side of the mucosa from deleterious 
      luminal agents.
FAU - Tomasetto, C
AU  - Tomasetto C
AD  - Institut de Genetique et de Biologie Moleculaire et Cellulaire (IGBMC),
      CNRS/INSERM Unite 184/ULP, Illkirch, France.
FAU - Masson, R
AU  - Masson R
FAU - Linares, J L
AU  - Linares JL
FAU - Wendling, C
AU  - Wendling C
FAU - Lefebvre, O
AU  - Lefebvre O
FAU - Chenard, M P
AU  - Chenard MP
FAU - Rio, M C
AU  - Rio MC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Gastroenterology
JT  - Gastroenterology
JID - 0374630
RN  - 0 (Growth Substances)
RN  - 0 (Mucins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Peptides)
RN  - 0 (RNA, Messenger)
RN  - 0 (TFF3 protein, rat)
RN  - 0 (Trefoil Factor-2)
RN  - 0 (Trefoil Factor-3)
RN  - 0 (von Willebrand Factor)
RN  - K848JZ4886 (Cysteine)
SB  - AIM
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Clone Cells
MH  - Cysteine
MH  - Duodenum/*metabolism
MH  - Gastric Mucosa/*metabolism
MH  - Growth Substances/*metabolism
MH  - Hybrid Cells
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mucins/chemistry/genetics/*metabolism
MH  - *Muscle Proteins
MH  - *Neuropeptides
MH  - Peptides/*metabolism
MH  - Protein Structure, Tertiary
MH  - RNA, Messenger/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Trefoil Factor-2
MH  - Trefoil Factor-3
MH  - Yeasts
MH  - von Willebrand Factor/genetics/*metabolism
EDAT- 1999/12/28 00:00
MHDA- 1999/12/28 00:01
CRDT- 1999/12/28 00:00
PHST- 1999/12/28 00:00 [pubmed]
PHST- 1999/12/28 00:01 [medline]
PHST- 1999/12/28 00:00 [entrez]
AID - S0016508500871589 [pii]
AID - 10.1016/s0016-5085(00)70415-x [doi]
PST - ppublish
SO  - Gastroenterology. 2000 Jan;118(1):70-80. doi: 10.1016/s0016-5085(00)70415-x.