Literature DB >> 25829151

cfMSP-1, an extremely acidic matrix protein involved in shell formation of the scallop Chlamys farreri.

Ganchu Jia1, Jian Liang1, Jun Xie1, Jun Wang1, Zhenmin Bao2, Liping Xie3, Rongqing Zhang4.   

Abstract

Matrix proteins play an important role in biomineralization by mollusks. In this study, we cloned and characterized an acidic protein (pI=3.36) homolog of cfMSP-1 that is highly expressed in the mantle transcriptome of the scallop Chlamys farreri. RT-PCR and in situ hybridization showed that cfMSP-1 is specifically expressed in the outer fold of the mantle edge and pallial part. The expression level of cfMSP-1 remarkably increased and then reduced gradually to a value that is ~2-fold higher than basal levels after shell notching. Knock-down expression of cfMSP-1 in adults via dsRNA injection gave a disordered folia surface. Both shell notching and RNAi experiments indicated that cfMSP-1 plays an essential role in the formation of the folia of C. farreri.
Copyright © 2015 Elsevier Inc. All rights reserved.

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Keywords:  Biomineralization; Chlamys farreri; Shell; cfMSP-1

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Year:  2015        PMID: 25829151     DOI: 10.1016/j.cbpb.2015.03.004

Source DB:  PubMed          Journal:  Comp Biochem Physiol B Biochem Mol Biol        ISSN: 1096-4959            Impact factor:   2.231


  1 in total

1.  fam20C participates in the shell formation in the pearl oyster, Pinctada fucata.

Authors:  Jinzhe Du; Chuang Liu; Guangrui Xu; Jun Xie; Liping Xie; Rongqing Zhang
Journal:  Sci Rep       Date:  2018-02-23       Impact factor: 4.379

  1 in total

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