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Last update 23 Jan 2025

GDF

Last update 23 Jan 2025

Basic Info

Synonyms

GD, GdA, GdF

+ [16]

Introduction

Glycoprotein that regulates critical steps during fertilization and also has immunomonomodulatory effects. Four glycoforms, namely glycodelin-S, -A, -F and -C have been identified in reproductive tissues that differ in glycosylation and biological activity. Glycodelin-A has contraceptive and immunosuppressive activities (PubMed:9918684, PubMed:7531163). Glycodelin-C stimulates binding of spermatozoa to the zona pellucida (PubMed:17192260). Glycodelin-F inhibits spermatozoa-zona pellucida binding and significantly suppresses progesterone-induced acrosome reaction of spermatozoa (PubMed:12672671). Glycodelin-S in seminal plasma maintains the uncapacitated state of human spermatozoa (PubMed:15883155).

Drugs associated with GDF

HS235

Target

GDF x activin receptor

Mechanism

GDF modulators [+1]

Active Org.

35Pharma, Inc.

Originator Org.

35Pharma, Inc.

Active Indication

Obesity

Inactive Indication-

Drug Highest PhasePhase 1

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

ACE-06X

Target

GDF

Mechanism

GDF modulators

Active Org.-

Originator Org.

Acceleron Pharma, Inc.

Active Indication-

Inactive Indication

Metabolic Diseases

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with GDF

NCT06714825

/ RecruitingPhase 1

Phase 1 Single and Multiple Ascending Dose Study in Males and Females Assessing the Pharmacokinetics, Safety, and Pharmacodynamics of HS235 in Overweight and Obese Otherwise Healthy Subjects

Study of HS235 for Assessing the Pharmacokinetics, Safety, and Pharmacodynamics of HS235 in Overweight and Obese Otherwise Healthy Subjects

Start Date28 Nov 2024

Sponsor / Collaborator

35Pharma, Inc.

100 Clinical Results associated with GDF

100 Translational Medicine associated with GDF

0 Patents (Medical) associated with GDF

1,246

Literatures (Medical) associated with GDF

01 Feb 2025·Biochemical and Biophysical Research Communications

Excessive BMP3b suppresses skeletal muscle differentiation

Article

Author: Kokabu, Shoichiro ; Ono, Yusuke ; Hino, Jun ; Miyawaki, Aki ; Tsuji, Kunikazu ; Kodama, Nao ; Matsubara, Takuma

Bone morphogenetic protein (BMP)-3b, also known as growth differentiation factor (GDF)-10, belongs to the transforming growth factor (TGF)-β superfamily. Despite being named a BMP, BMP3b is considered as an intermediate between the TGFβ/activin/myostatin and BMP/GDF subgroups of the TGFβ superfamily. Myoblast differentiation is tightly regulated by various cytokines, including the TGFβ superfamily members. However, despite BMP3b supporting the maintenance of skeletal myofibers, myoblast differentiation induced by BMP3b remains unclear. In this study, BMP3 expression levels in isolated satellites were very low compared to those in the skeletal muscle tissues. We analyzed cardiotoxin-induced muscle regeneration. Intact muscle fiber size was larger in BMP3b null mice than in wild-type mice; however, regenerated muscle fiber size did not differ between the null and wild-type mice. Next, we analyzed the satellite cell-specific BMP3b-overexpressing (BMP3b Tg) mice. Intact fiber size was increased in BMP3b Tg mice. However, regenerating tibialis anterior muscle size was reduced in BMP3b Tg mice compared to that in control mice. BMP3b overexpression in C2C12 cells stimulated Smad2/3 signaling. Moreover, BMP3b overexpression and conditioned medium of BMP3b-expressing Chinese hamster ovary cells strongly suppressed myoblast differentiation by repressing transactivation. Overall, our data suggest that BMP3b is not necessary for muscle regeneration; however, excessive BMP3b interferes with muscle regeneration by suppressing myoblast differentiation.

01 Jan 2025·The Plant Journal

GhTBL3 is required for fiber secondary cell wall (SCW) formation via maintaining acetylation of xylan in cotton

Article

Author: Cheng, Chang‐Hao ; Zou, Dan ; Li, Xue‐Bao ; Zheng, Yong ; Zhang, Jie ; Zhang, Jing‐Bo ; Wang, Yao ; Li, Yang

SUMMARYTBL family proteins containing the domain of unknown function mainly act as xylan O‐acetyltransferases, but the specific molecular mechanism of their functions remains unclear in plants (especially in cotton) so far. In this study, we characterized the TBL family proteins containing the conserved GDS and DxxH motifs in cotton (Gossypium hirsutum). Among them, GhTBL3 is highly expressed in fibers at the stage of secondary cell wall (SCW) formation and mainly functions as O‐acetyltransferase to maintain acetylation of xylan in fiber SCW development. Overexpression of GhTBL3 in cotton promoted fiber SCW formation, resulting in increased fiber cell wall thickness. In contrast, suppression of GhTBL3 expression in cotton impaired fiber SCW synthesis, leading to the decreased fiber cell wall thickness, compared with wild type (WT). Furthermore, two fiber SCW‐related transcription factors GhMYBL1 and GhKNL1 were found to directly bind to the promoter of GhTBL3 in cotton. GhMYBL1 enhanced the transcription activity of GhTBL3, whereas GhKNL1 inhibited the expression of GhTBL3 in fibers. The acetylation level of xylan was remarkably decreased in fibers of GhMYBL1 RNAi transgenic cotton, but the acetylation level of xylan was significantly increased in fibers of GhKNL1 RNAi cotton, relative to WT. Given together, the above results suggested that GhTBL3 may be under the dual control of GhMYBL1 and GhKNL1 to maintain the suitable acetylation level of xylan required for fiber SCW formation in cotton. Thus, our data provide an effective clue for potentially improving fiber quality by genetic manipulation of GhTBL3 in cotton breeding.

01 Dec 2024·Cellular Signalling

Acyl-CoA long-chain synthetase 1 (ACSL1) protects the endometrium from excess palmitic acid stress during decidualization

Article

Author: Wang, Xinyu ; Zhou, Feng ; Zeng, Biya ; Zhang, Songying ; Liu, Na ; Zhang, Yi ; Sun, Fangying ; Lin, Xiang ; Zhao, Fanxuan ; Dai, Yongdong ; Gu, Weijia

Endometrial receptivity relies on the functional and morphological change of endometrium stromal cells (EnSCs) and epithelial cells in the secretory phase. Decidualization of ESCs and transitions in endometrium epithelial cells are crucial for successful uterine implantation and maintaining pregnancy. Accumulated data have demonstrated that decidualization is tightly coordinated by lipid metabolism. However, the lipidomic change and regulatory mechanism in uterine decidualization are still unknown. Our study showed that endometrium stromal cells and decidual stromal cells had different lipidomic profiles. Acyl-CoA long-chain synthetase 1 (ACSL1) which converts fatty acids to acyl-CoA expression was strongly elevated during decidualization. ACSL1 knockdown inhibited stromal-to-decidual cell transition and decreased the decidualization markers prolactin and Insulin-like growth factor-binding protein-1 (IGFBP1) expression through the AKT pathway. Lipid uptake was upregulated in stromal cells while lipid droplet accumulation was downregulated during decidualization. Meanwhile, silencing of ACSL1 led to impaired spare respiratory capacity, and downregulation of TFAM expression, indicating robust lipid metabolism. While palmitic acid addition impeded decidualization, overexpression of ACSL1 could partially reverse its effect. ACSL inhibitor Triacsin C significantly impeded decidualization in a three-dimensional coculture model consisting of endometrial stromal cells and epithelial cells. Knockdown of ACSL1 in stromal cells decreased the expression of the decidualization markers PAEP and SPP1 in epithelial cells. Collectively, ACSL1 is essential for uterine decidualization and protects stromal cells from excess palmitic acid stress.

News (Medical) associated with GDF

28 Nov 2024

·www.globenewswire.com

35Pharma Closes Series C Financing to Advance Clinical Pipeline of Activin Inhibitors for Pulmonary Hypertension, Cardiometabolic Disease and Obesity

Financing led by Frazier Life Sciences with participation from new investors including Vivo Capital, Janus Henderson Investors, Deep Track Capital, Paradigm BioCapital Advisors and Columbia Threadneedle Nov. 26, 2024 -- 35Pharma, a clinical-stage biopharmaceutical company developing TGF-beta superfamily therapeutics, today announced the closing of an oversubscribed $53 million Series C financing. The company plans to use the proceeds to advance its pipeline of Activin and GDF inhibitors, HS135 for pulmonary hypertension and HS235 for cardiometabolic disease and obesity. The Series C financing was led by Frazier Life Sciences with participation from additional new investors that included Vivo Capital, Janus Henderson Investors, Deep Track Capital, Paradigm BioCapital Advisors, Columbia Threadneedle, as well as from existing investors VenBio, Surveyor Capital, Logos Capital and Marshall Wace. "We are delighted to close this Series C financing, which brings multiple new marquee healthcare investors into our cap table," said Ilia A. Tikhomirov, CEO of 35Pharma. "This financing is intended to support initial clinical proof-of-concept studies for HS135 in pulmonary hypertension, as well as advance HS235 - our candidate for the treatment of HFpEF and obesity - through a Phase 1 proof-of-biology trial in obese and overweight healthy volunteers." "Targeting Activin- and GDF-mediated signaling has emerged as an important therapeutic approach across cardiometabolic and pulmonary disease," said Kevin Li, M.D., Principal at Frazier Life Sciences. "Drawing from its deep expertise in TGF-beta biology and protein engineering, 35Pharma has developed two clinical-stage assets with the potential for best-in-class efficacy and safety. Frazier Life Sciences is pleased to support the team in advancing their pipeline through the clinic, and toward the goal of transforming the standard of care in pulmonary hypertension, obesity, and heart failure." 35Pharma is a clinical-stage biopharmaceutical company focused on developing best-in-class transforming growth factor-beta (TGF-beta) superfamily ligand traps for pulmonary hypertension, obesity and cardiometabolic diseases. 35Pharma leverages its scientific leadership in TGF-beta biology, combined with superior protein engineering, to discover innovative compounds that selectively and potently neutralize validated pathological TGF-beta superfamily ligands, while sparing beneficial homeostatic ligands. For more information, please visit www.35pharma.com The content above comes from the network. if any infringement, please contact us to modify.

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