Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 Å resolution: a bovine polypeptide of the spermadhesin family

Romão, Maria João; Kölln, Ingo; Dias, João M.; Carvalho, Ana Luı́sa; Romero, Antonio; Varela, Paloma F.; Sanz, Libia; Töpfer‐Petersen, Edda; Calvete, Juan J.

doi:10.1006/jmbi.1997.1423

Cited by 40 publications

(17 citation statements)

References 21 publications

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“…CUB domains are assembled as a PDGF-C and -D, structure and function compact ellipsoidal b-sandwich, with a hydrophobic core essential for the overall domain folding. The b-sandwich is built up of two five-stranded b-sheets of antiparallel b-strands [33][34][35][36]. Most CUB domains are reported to contain four conserved cysteines that form two disulfide bridges between nearest-neighbour cysteines, resulting in disulfide bridges located on opposite edges of the domain.…”

Section: The Cub Domain Of Pdgf-c and Pdgf-dmentioning

confidence: 99%

Structural and functional specificities of PDGF‐C and PDGF‐D, the novel members of the platelet‐derived growth factors family

2005

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The platelet‐derived growth factor (PDGF) family was for more than 25 years assumed to consist of only PDGF‐A and ‐B. The discovery of the novel family members PDGF‐C and PDGF‐D triggered a search for novel activities and complementary fine tuning between the members of this family of growth factors. Since the expansion of the PDGF family, more than 60 publications on the novel PDGF‐C and PDGF‐D have been presented, highlighting similarities and differences to the classical PDGFs. In this paper we review the published data on the PDGF family covering structural (gene and protein) similarities and differences among all four family members, with special focus on PDGF‐C and PDGF‐D expression and functions. Little information on the protein structures of PDGF‐C and ‐D is currently available, but the PDGF‐C protein may be structurally more similar to VEGF‐A than to PDGF‐B. PDGF‐C contributes to normal development of the heart, ear, central nervous system (CNS), and kidney, while PDGF‐D is active in the development of the kidney, eye and brain. In adults, PDGF‐C is active in the kidney and the central nervous system. PDGF‐D also plays a role in the lung and in periodontal mineralization. PDGF‐C is expressed in Ewing family sarcoma and PDGF‐D is linked to lung, prostate and ovarian cancers. Both PDGF‐C and ‐D play a role in progressive renal disease, glioblastoma/medulloblastoma and fibrosis in several organs.

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Section: The Cub Domain Of Pdgf-c and Pdgf-dmentioning

confidence: 99%

Structural and functional specificities of PDGF‐C and PDGF‐D, the novel members of the platelet‐derived growth factors family

2005

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“…At the protein level, the e2770 mutation maps to the CUB domain, which is a protein-protein interaction pattern formation in Drosophila (Marqués et al 1997). Mammalian BMP-1 is a major ECM regulator, which, in module composed of 10 ␤-strands arranged in a jellyrolltype topology (Romão et al 1997). The Pro substitution addition to its key role in the BMP-signaling pathway, affects the consensus sequence of ␤-strand 9, thus potendpy-31 occasionally resulted in an embryonic lethal phenotype in the progeny similar to that exhibited by dpy-31 tially leading to the disruption of the CUB domain fold.…”

Section: Construction Of a Line Carrying The E2770 Mutationmentioning

confidence: 99%

Gene Interactions in Caenorhabditis elegans Define DPY-31 as a Candidate Procollagen C-Proteinase and SQT-3/ROL-4 as Its Predicted Major Target

2004

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Zinc metalloproteases of the BMP-1/TOLLOID family (also known as astacins) are extracellular enzymes involved in important developmental processes in metazoans. We report the characterization of the Caenorhabditis elegans gene dpy-31, which encodes the first essential astacin metalloprotease identified in this organism. Loss-of-function mutations in dpy-31 result in cuticle defects, abnormal morphology, and embryonic lethality, indicating that dpy-31 is required for formation of the collagenous exoskeleton. DPY-31 is widely expressed in the hypodermal cells, which are responsible for cuticle secretion. We have investigated the dpy-31 function through reversion analysis. While complete reversion can be obtained only by intragenic suppressors, reversion of the Dpy-31 lethal phenotype also can be caused by dominant extragenic suppressors. Nine extragenic suppressors carry mutations in the uniquely essential collagen gene sqt-3, which we show is the same gene as rol-4. Most mutations exhibit the unusual property of exclusively dominant suppression and all affect the sequence of the SQT-3 collagen C terminus. This suggests that DPY-31 is responsible for C-terminal proteolytic processing of collagen trimers and is therefore a structural and functional homolog of vertebrate BMP-1. The results also demonstrate the critical importance of the collagen C-terminal sequence, which is highly conserved among all 49 members of the SQT-3 subfamily.

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“…Another seminal plasma molecule known as acidic seminal fluid protein (aSFP) also has actions on the control of oxidative stress in the bovine reproductive tract (Einspanier et al, 1993;Schöneck et al, 1996). aSFP shares identity with molecules of spermadhesin family (Romão et al, 1997) and, in the bull, it is secreted by both the epididymides and accessory sex glands (Moura et al, 2007a(Moura et al, , 2010. Binding of aSFP to ejaculated sperm occurs but it is lost after capacitation (Dòstolovà et al, 1994), suggesting that, unlike porcine spermadhesins (Caballero et al, 2004(Caballero et al, , 2005, bovine aSFP does not participate in spermoocyte interaction.…”

Section: Proteins Involved In Sperm Protectionmentioning

confidence: 99%

Functional aspects of seminal plasma and sperm proteins and their potential as molecularmarkers of fertility

Moura

Memili

2016

Anim Reprod

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Molecular components of sperm and in the media surrounding them influence bull fertility. Given this concept, proteins of the seminal plasma modulate crucial functions and events of reproduction, such as sperm motility and capacitation, cell protection, acrosome reaction, fertilization and embryonic development. Sperm proteins are also important for successful fertilization, egg activation and embryo development. Empirical associations between seminal and sperm proteins and fertility in the bovine indicate that these proteins are potential molecular markers of the male reproductive status.

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Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 Å resolution: a bovine polypeptide of the spermadhesin family

Cited by 40 publications

References 21 publications

Structural and functional specificities of PDGF‐C and PDGF‐D, the novel members of the platelet‐derived growth factors family

Structural and functional specificities of PDGF‐C and PDGF‐D, the novel members of the platelet‐derived growth factors family

Gene Interactions in Caenorhabditis elegans Define DPY-31 as a Candidate Procollagen C-Proteinase and SQT-3/ROL-4 as Its Predicted Major Target

Functional aspects of seminal plasma and sperm proteins and their potential as molecularmarkers of fertility

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