GH2

Last update 08 May 2025

Basic Info

Synonyms

GH-V, GH2, GHL

+ [5]

Introduction

Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.

100 Clinical Results associated with GH2

100 Translational Medicine associated with GH2

0 Patents (Medical) associated with GH2

375

Literatures (Medical) associated with GH2

24 Mar 2025·Endocrinology

Evolution of the Complex Growth Hormone Gene Cluster in Macaques

Article

Author: Wallis, Michael

AbstractIn higher primates, unlike other mammals, the GH gene locus is complex, comprising several GH-like genes, resulting from gene duplication and divergent evolution, expressed in pituitary and placenta. There are 5 genes in this GH gene cluster in human and 5 to 7 in apes and most Old-World monkeys, but in macaques the cluster has expanded further. Here the nature and evolution of the GH locus in this important primate genus is explored. Analysis of genomic data for Macaca fascicularis (crab-eating macaque) revealed that the GH gene cluster in this species is variable, with at least 5 different haplotypes, comprising 11 to 14 GH-like genes. Gene-number heterozygosity was also detected in Macaca mulatta (rhesus macaque) with 9 to 13 genes. Analysis of genomic data for other macaque species revealed GH gene clusters containing 8 to 14 GH-like genes, but gene-number heterozygosity was not detected. Expression of GH-like genes in pituitary and placenta was examined for Macaca fascicularis. This analysis has established that the complexity of the GH gene cluster increased during the evolution of macaques, by gene duplication and divergent evolution, and that these processes continue within at least 2 extant species. Analysis of rate of sequence change, and distribution of substitutions within the 3D structure, shows that for at least 1 GH-like gene (GH2), the changes reflect positive selection, implying adaptive biological change. Whether this involves changes in physiological (endocrine) function or response to viral or other pathogenic challenge is not yet clear.

01 Jan 2025·Fish & Shellfish Immunology

Host-intestinal microbiota interactions in Edwardsiella piscicida-induced lethal enteritis in big-belly seahorses: Novel insights into the role of Carbohydrate-Active enzymes and host transcriptional responses

Article

Author: Li, Lin ; Wang, Kai ; Xue, Yuanyuan ; Zheng, Shiyi ; Su, Xiaolei ; Zhang, Jingyi ; Zhang, Lele ; Yang, Hongwei ; Jia, Longwu ; Ma, Yicong ; Li, Mingzhu

Edwardsiella piscicida-induced lethal enteritis is a major threat to the sustainable development of seahorse aquaculture. The roles of Carbohydrate-Active enzymes (CAZymes) in interactions between the pathogen and the host are poorly understood. In this study, we found that 22 key CAZymes encoded by E. piscicida might involve in the coordination of five key stages of infection. Specifically, during the motility, adherence, and invasion stages, 10 CAZymes, including CE4, PL8, and CBM48, may significantly increase the activities of Lipid metabolism-associated pathways of the intestinal microbiota (P < 0.01), facilitating pathogen invasion of the host intestinal epithelium. During the replication stage, 11 CAZymes, including GH20, GT4, and GH3, may significantly increase activities of pathways associated with Carbohydrate metabolism (P < 0.01) to promote replication and proliferation of the pathogen. And for avoiding host defenses, GH2 and GH1 may enhance activities of both Carbohydrate and Amino acid metabolic pathways (P < 0.01), facilitating infection and immune evasion. Conjoint analysis showed that E. piscicida might mainly rely on Carbohydrate metabolism for infection, while the host might activate Amino acid metabolic pathways for self-defense. In addition, expressions of 10 key genes, Aldh9a1b, Aoc1, Tpi1b, PCK1, Ldha, Me1, Gla, Cel.2, Ugdh, and Mao, were significantly altered (P < 0.01) and may be used for characterizing host responses to E. piscicida infection. Activities of both Glycolysis/Gluconeogenesis and Tryptophan metabolism were found oppositely changed (P < 0.01) between pathogen and host, respectively, representing the primary focuses of the competition. Overall, this study provides new insights into E. piscicida-mediated intestinal enteritis in fish for the first time from the perspective of CAZymes, as well as a theoretical reference for the prevention and control of these diseases in the aquaculture of seahorses and other fish.

01 Dec 2024·FEBS Letters

Crystal structure of β‐d‐galactofuranosidase from Streptomyces sp. JHA19 in complex with an inhibitor provides insights into substrate specificity

Article

Author: Matsunaga, Emiko ; Nash, Robert J. ; Kashima, Toma ; Takegawa, Kaoru ; Fushinobu, Shinya ; Fujio, Noriki ; Yamada, Chihaya

d‐Galactofuranose (Galf) is widely distributed in glycoconjugates of pathogenic microbes. β‐d‐Galactofuranosidase (Galf‐ase) from Streptomyces sp. JHA19 (ORF1110) belongs to glycoside hydrolase (GH) family 2 and is the first identified Galf‐specific degradation enzyme. Here, the crystal structure of ORF1110 in complex with a mechanism‐based potent inhibitor, d‐iminogalactitol (Ki = 65 μm) was solved. ORF1110 binds to the C5–C6 hydroxy groups of d‐iminogalactitol with an extensive and integral hydrogen bond network, a key interaction that discriminates the substrates. The active site structure of ORF1110 is largely different from those of β‐glucuronidases and β‐galactosidases in the same GH2 family. A C‐terminal domain of ORF1110 is predicted to be a carbohydrate‐binding module family 42 that may bind Galf. The structural insights into Galf‐ase will contribute to the investigation of therapeutic tools against pathogens.

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GH2

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