Proteomic analysis of shell matrix proteins from the chiton Acanthopleura loochooana.
Comp Biochem Physiol Part D Genomics Proteomics
; 49: 101176, 2024 Mar.
Article
in En
| MEDLINE
| ID: mdl-38128379
ABSTRACT
Most molluscs have mineralized shells to protect themselves. Although the remarkable mechanical properties of shells have been well-studied, the origin of shells is still elusive. Chitons are unique in molluscs because they are shelly Aculifera which diverged from Conchifera (comprising all the shell-bearing classes of molluscs) in the early pre-Cambrian. We developed a method to extract shell proteins from chiton shell plates (removing embedded soft tissues) and then compared the shell proteome to that of Conchifera groups. Sixteen shell matrix proteins from Acanthopleura loochooana were identified by proteomics, in which Nacrein-like, Pif-like proteins, and protocadherin were found. Additional evidences from shell proteome in another species Chiton densiliratus and comparative sequence alignment in five chitons supported a conserved biomineralization toolkit in chitons. Our findings shed light on the evolution of mineralization in chitons and pose a hypothesis that ancestral molluscs have already evolved biomineralization toolkits, which may facilitate the formation of mineralized shells.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Polyplacophora
Limits:
Animals
Language:
En
Journal:
Comp Biochem Physiol Part D Genomics Proteomics
Journal subject:
BIOLOGIA
/
GENETICA
Year:
2024
Type:
Article