A Crayfish Insulin-like-binding Protein

Rosen, Ohad; Weil, Shalva; Manor, Rivka; Roth, Ziv; Khalaila, Isam; Sagi, Amir

doi:10.1074/jbc.m113.484279

Cited by 50 publications

(26 citation statements)

References 54 publications

(66 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The interaction between crustacean IGFBP and IAG was first demonstrated in C. quadricarinatus (Rosen et al, 2013). In this study, we verified the interaction between EsIGFBP7 and EsIAG using a yeast-two hybrid assay.…”

Section: Discussionsupporting

confidence: 56%

“…Although the IGFBP family has many members in vertebrates, only one member has been identified in crustacean species, until now (Rosen et al, 2013;Li et al, 2015). Crustacean IGFBPs are most homologous with vertebrate IGFBP7, and they share a common structural organization of an IB domain in the N-terminus, a KAZAL domain in the middle, and an IG domain in the C-terminus.…”

Section: Discussionmentioning

confidence: 99%

“…Members of the insulinlike growth factor binding proteins (IGFBPs) can bind insulin/insulin-like growth factor, so it was speculated that an interaction between IAG and insulin-like growth factor binding protein (IGFBP) product had occurred (Manor et al, 2007). In 2013, researchers discovered that IAG gene interact with IGFBP gene products in the crayfish, Cherax quadricarinatus, which provided new clues to study the function of the crustacean AG pathway (Rosen et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Untitled

Song¹,

Xu²,

Zang³

et al. 2018

Turk. J. Fish. Aquat. Sci.

View full text Add to dashboard Cite

Androgenic gland hormone has an insulin-like structure and it is the male-specific hormone found in crustaceans. Androgenic gland hormone controls male sexual differentiation and maintains male sexual characteristics. In this study, the full-length cDNA sequence of the androgenic gland hormone gene in Eriocheir sinensis (EsIAG) was cloned. The total length of the EsIAG cDNA was 1,495 bp, encoding 151 amino acids. EsIAG has the typical conserved structure of other reported IAGs but had low sequence similarity with other crustacean IAGs. EsIAG was expressed specifically in the androgenic gland. Insulin-like growth factor binding protein 7 from the Chinese mitten crab E. sinensis (EsIGFBP7) was highly expressed in the male sex-related organs among nine crab tissues. Interactions between EsIAG and EsIGFBP7 were verified using a yeast-two hybrid assay. These results obtained in this study provide basic information about the regulatory mechanism of male sex differentiation in E. sinensis.

show abstract

Section: Discussionsupporting

confidence: 56%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Untitled

Song¹,

Xu²,

Zang³

et al. 2018

Turk. J. Fish. Aquat. Sci.

View full text Add to dashboard Cite

show abstract

“…IAG is known to regulate male sexual development, specifically secondary sexual features and spermatogenesis, suggesting that the levels of IAG expression in the AG and of the hemolymph IAG titers may be closely associated with male sexual maturity. It is reported that IAG requires a binding partner, an insulin-like binding protein, or an insulin-like binding protein like peptide [ 24 ]. The exact mode of the IAG mechanism by which it regulates such processes still remains to be studied.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Tissue Distribution of an Insulin-Like Androgenic Gland Hormone (IAG) of the Male Red Deep-Sea Crab, Chaceon quinquedens

2017

View full text Add to dashboard Cite

The insulin-like androgenic gland hormone (IAG) found in decapod crustaceans is known to regulate sexual development in males. IAG is produced in the male-specific endocrine tissue, the androgenic gland (AG); however, IAG expression has been also observed in other tissues of decapod crustacean species including Callinectes sapidus and Scylla paramamosain. This study aimed to isolate the full-length cDNA sequence of IAG from the AG of male red deep-sea crabs, Chaceon quinquedens (ChqIAG), and to examine its tissue distribution. To this end, we employed polymerase chain reaction cloning with degenerate primers and 5′ and 3′ rapid amplification of cDNA ends (RACE). The full-length ChqIAG cDNA sequence (1555 nt) includes a 366 nt 5′ untranslated region a 453 nt open reading frame encoding 151 amino acids, and a relatively long 3′ UTR of 733 nt. The ORF consists of a 19 aa signal peptide, 32 aa B chain, 56 aa C chain, and 44 aa A chain. The putative ChqIAG amino acid sequence is most similar to those found in other crab species, including C. sapidus and S. paramamosain, which are clustered together phylogenetically.

show abstract

“…The same species of diatoms were tested in other times [15] or on other decapods [25] but they did not elicit any bioactivity comparable to the one detected on young post-larvae of H. inermis . Additionally, toxicity tests performed with crude extracts of the diatom C. scutellum parva on embryos of the sea urchin Paracentrotus lividus did not elicit any significant effects [26].…”

Section: Introductionmentioning

confidence: 99%

Apoptogenic Metabolites in Fractions of the Benthic Diatom Cocconeis scutellum parva

et al. 2014

View full text Add to dashboard Cite

Benthic diatoms of the genus Cocconeis contain a specific apoptogenic activity. It triggers a fast destruction of the androgenic gland in the early post-larval life of the marine shrimp Hippolyte inermis, leading to the generation of small females. Previous in vitro investigations demonstrated that crude extracts of these diatoms specifically activate a dose-dependent apoptotic process in human cancer cells (BT20 breast carcinoma) but not in human normal lymphocytes. Here, a bioassay-guided fractionation has been performed to detect the apoptogenic compound(s). Various HPLC separation systems were needed to isolate the active fractions, since the apoptogenic metabolite is highly active, present in low amounts and is masked by abundant but non-active cellular compounds. The activity is due to at least two compounds characterized by different polarities, a hydrophilic and a lipophilic fraction. We purified the lipophilic fraction, which led to the characterization of an active sub-fraction containing a highly lipophilic compound, whose molecular structure has not yet been identified, but is under investigation. The results point to the possible medical uses of the active compound. Once the molecular structure has been identified, the study and modulation of apoptotic processes in various types of cells will be possible.

show abstract

A Crayfish Insulin-like-binding Protein

Cited by 50 publications

References 54 publications

Untitled

Untitled

Isolation and Tissue Distribution of an Insulin-Like Androgenic Gland Hormone (IAG) of the Male Red Deep-Sea Crab, Chaceon quinquedens

Apoptogenic Metabolites in Fractions of the Benthic Diatom Cocconeis scutellum parva

Contact Info

Product

Resources

About