Chordin

Source: Wikipedia, the free encyclopedia.
CHRD domain
Identifiers
SymbolCHRD
PfamPF07452
InterProIPR010895
SMARTSM00754
PROSITEPS50933
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
chordin
Identifiers
SymbolCHRD
Chr. 3 q27
Search for
StructuresSwiss-model
DomainsInterPro

Chordin (from Greek χορδή, string, catgut) is a protein with a prominent role in dorsal–ventral patterning during early embryonic development. In humans it is encoded for by the CHRD gene.[1][2]

History

Chordin was originally identified in the

gsc and Xnot were also expressed, which included the prechordal plate, the notochord, and the chordoneural hinge
. The expression of the gene in these regions led to the name chordin. Initial functions of chordin were thought to include recruitment of neighboring cells to assist in the forming of the axis along with mediating cell interactions for organization of tail, head, and body regions.

Protein Structure

Chordin is a 941 amino-acids long protein, whose three-dimensional

isoforms of this protein that are produced by alternative splicing.[8]

Gene structure

CHRD is 23 exons long and has a length of 11.5 kb and is localized at 3q27.[1][9] The THPO (thrombopoietin) gene is located in the same single cosmid clone along with the eukaryotic translation initiation factor-4-gamma gene (EIF4G1).[2]

Function

Chordin

TGFβ proteins such as bone morphogenetic proteins (BMP) through its four cytosine rich regions.[7][9] Chordin blocks BMP signaling by preventing BMP from interacting with cell surface receptors, which inhibits the formation of epidermis and promoting the formation of neural tissue.[10] Chordin specifically inhibits BMP-2,-4,-7.[6] Chordin function is improved by a few co-factors that include the Twisted Gastrulation gene (Tsg) and the zinc metalloprotease. Tsg improves the ability of Chordin to become a BMP antagonist. Zinc metalloprotease functions by cleaving chordin allows for improved signaling with BMP in complexes that were inactive. This occurs by improving Chordin's substrate ability in cleavage reactions and by releasing BMP from chordin products.[7]

Experiments with zebrafish showed that a chordin gene mutation can lead to less neural and dorsal tissue. Target gene deletions of chordin,

anterior visceral endoderm.[13]

Chordin mRNA in mice are expressed early on during the anterior primitive streak. In the chick embryo it is expressed in the anterior cells of Koller's sickle, which form the anterior cells of the primitive streak, a key structure through which gastrulation occurs.[14] As the streak evolves to a node and axial mesoderm, the chordin mRNA is still expressed. This evidence suggests a patterning role of chordin during the early embryo stages.[13] When chordin was inactivated, animals may initially appear to have normal development, but later on issues manifest in the inner and outer ear along with pharyngeal and cardiovascular abnormalities. Experiments with Xenopus embryos showed that overexpression of BMP1 and TLL1 can be used to counteract chordin's dorsalization functions. This finding suggests that the major chordin antagonist is BMP1.[1]

In mice, chordin is expressed in the node but not in the anterior visceral endoderm. It has been found to be required for forebrain development.[13] In developing mice that are deficient in both chordin and noggin, the head is nearly absent. Chordin is also involved in avian gastrulation and may also play a role in organogenesis.

References

  1. ^
    PMID 10479448
    .
  2. ^
    PMID 10480362
    .
  3. PMID 8001117
    .
  4. ^ "Not.S - Xnot protein - Xenopus laevis (African clawed frog) - not.S gene & protein".
  5. PMID 10648240
    .
  6. ^
    PMID 26517884
    .
  7. ^
    ISBN 978-3-662-10416-3
    .
  8. S2CID 16208655
    .
  9. ^
    PMID 9782094
    .
  10. PMID 24284174
    .
  11. ISBN 978-0-08-047249-2
    .
  12. ISBN 978-0-12-374539-2
    .
  13. ^
    S2CID 11212713
    .
  14. PMID 20485500
    .
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