Molecular cloning and functional analysis of the fatty acid-binding protein (Sp-FABP) gene in the mud crab (Scylla paramamosain)

نویسندگان

  • Xianglan Zeng
  • Haihui Ye
  • Ya’nan Yang
  • Guizhong Wang
  • Huiyang Huang
چکیده

Intracellular fatty acid-binding proteins (FABPs) are multifunctional cytosolic lipid-binding proteins found in vertebrates and invertebrates. In this work, we used RACE to obtain a full-length cDNA of Sp-FABP from the mud crab Scylla paramamosain. The open reading frame of the full length cDNA (886 bp) encoded a 136 amino acid polypeptide that showed high homology with related genes from other species. Real-time quantitative PCR identified variable levels of Sp-FABP transcripts in epidermis, eyestalk, gill, heart, hemocytes, hepatopancreas, muscle, ovary, stomach and thoracic ganglia. In ovaries, Sp-FABP expression increased gradually from stage I to stage IV of development and decreased in stage V. Sp-FABP transcripts in the hepatopancreas and hemocytes were up-regulated after a bacterial challenge with Vibrio alginnolyficus. These results suggest that Sp-FABP may be involved in the growth, reproduction and immunity of the mud crab.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Molecular cloning, characterization and expression analysis of heat shock protein 90 (HSP90) from the mud crab Scylla paramamosain

Heat shock protein 90 (HSP90) is a highly conserved protein and plays an important role in maintaining the structure of protein, participating in the immunity and regulating the cell cycle. Using the rapid amplification of cDNA ends (RACE) techniques, the cDNA sequence of HSP90 gene (designated SpHSP90) was cloned and characterized from the mud crab Scylla paramamosain. The full-length cDNA of ...

متن کامل

cDNA Cloning and Expression of Translationally Controlled Tumour Protein (TCTP) Isolated from Mud Crab Scylla paramamosain in Escherichia coli

Translationally controlled tumour proteins (TCTP) cDNA were cloned from the haemolymph of Scylla paramamosain by reverse transcription PCR using primers derived from Penaeus monodon. Nucleotide sequence analysis revealed 507 bp open reading frame (ORF) encoding 168 amino acid residues with a predicted molecular mass and pI of approximately 19.2 kDa and 4.5, respectively. Interestingly, mud crab...

متن کامل

Characterization and expression analysis of chymotrypsin after bacterial challenge in the mud crab, Scylla paramamosain

Chymotrypsin is one of the serine proteases families that have various biological functions. A chymotrypsin gene was isolated from hepatopancreas of the mud crab, Scylla paramamosain (designated SpCHY) in this study. The full-length cDNA of SpCHY contained 942 nucleotides with a polyadenylation sequence and encoded a peptide of 270 amino acids with a signal peptide of 17 amino acids. The SpCHY ...

متن کامل

Cloning and characterization of the SpLRR cDNA from green mud crab, Scylla paramamosain.

Infectious diseases have seriously inhibited the aquaculture of mud crab Scylla paramamosain in southeastern China. Identification of the immune molecules and characterization of the defense mechanisms will be pivotal to the reduction of these diseases. Available data show that leucine-rich repeat (LRR) proteins play a crucial role in protein-protein interactions, recognition processes or immun...

متن کامل

Molecular cloning and expression profiles of nitric oxide synthase (NOS) in mud crab Scylla paramamosain.

The importance of the nitric oxide synthase (NOS) gene family is demonstrated by many studies in vertebrates and invertebrates in recent years. However, it keeps unknown of nitric oxide (NO) system and NOS gene family in mud crab Scylla paramamosain, an important cultured commercial crustacean in China and Pacific area. In this report, the cDNA of NOS containing full-length ORF was cloned from ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 36  شماره 

صفحات  -

تاریخ انتشار 2013