Disease relevance of Sycp1

• Dehydration with glycerol alone resulted in clumping of chromatin and loss of SC structure, histone solubility and histone-DNA linkages [1].
• SCP-1 can stimulate the contraction of isolated guinea pig ileum and SCP-2 induces hypotension in anesthetized rat [2].

High impact information on Sycp1

• In meiotic prophase, the sister chromatids of each chromosome develop a common axial element (AE) that is integrated into the synaptonemal complex (SC) [3].
• Mammalian protein SCP1 forms synaptonemal complex-like structures in the absence of meiotic chromosomes [4].
• We conclude that SCP1 is a primary determinant of SC assembly that plays a key role in synapsis of homologous chromosomes [4].
• To investigate the role of SCP1 in SC assembly, we expressed SCP1 in a heterologous system, i.e., in COS-7 cells that normally do not express SC proteins [4].
• The amino acid sequence of this polypeptide with a SDS-PAGE mobility corresponding to M(r) 145,000 has been deduced from a cDNA clone isolated from a Xenopus laevis ovary expression library and defines a polypeptide of 977 amino acids with a calculated mass of 111 kDa, with partial sequence homology to a synaptonemal complex protein, SCP2 [5].

Chemical compound and disease context of Sycp1

• Partial dehydration to a fifty percent concentration with these three solvents followed by freeze substitution with ethanol resulted in the loss of SC structure and histone solubility but the preservation of histone-DNA linkages [1].
• Dehydration with ethylene gylcol or hexylene glycol resulted in preservation of SC with a clear delineation of attachment of the chromatin fibrils to the lateral elements, but a loss of histone solubility and histone-DNA linkages [1].

Biological context of Sycp1

• SCP1-deficient ovaries exhibited an increased number of newly formed follicles, suggesting that completion of meiotic prophase I endows oocytes with the ability to orchestrate follicular assembly [6].
• Temporal and spatial control of the Sycp1 gene transcription in the mouse meiosis: regulatory elements active in the male are not sufficient for expression in the female gonad [7].
• Constructs with Sycp1 5' upstream sequences directed the expression of reporter genes to pachytene spermatocytes in transgenic mice [7].
• Extracts from cells that have reached metaphase I upon okadaic acid treatment, with concomitant displacement of SYN1/SCP1 and COR1/SCP3 from their chromosomes, do not have this capability [8].
• These data support the hypothesis that phosphorylation of SYN1/SCP1 and COR1/SCP3 targets their removal from the chromosomes and that activity of the kinases involved correlates with the presence of these two proteins on the chromosomes [8].

Anatomical context of Sycp1

• In developing rat ovaries, SCP1 mRNA expression is confined to oocytes and decreases precipitously within 24 h after birth, preceding the organization of primordial follicles [6].
• One of them encodes synaptonemal complex protein-1 (SCP1), a core component of the protein complex that maintains recombining chromosomes together during prophase I of the first meiotic division in germ cells [6].
• Substantial evidence supports the hypothesis that SCP1 operates as a noncatalytic carrier protein for the water-insoluble substrate squalene in the enzymatic conversion of squalene to lanosterol by liver microsomal membranes [9].
• SCP1 was catalytically inactive when it was incubated with [3H] squalene and cofactors in the absence of microsomes [9].
• X-ray-induced synaptonemal complex damage during meiotic prophase in female fetuses of Rattus norvegicus [10].

Associations of Sycp1 with chemical compounds

• The Km observed for SCP1 was similar to the Km observed for squalene [9].
• The formation of lanosterol was a hyperbolic function of the concentration of SCP1 present in the incubation mixture [9].
• Interestingly, the expression pattern of lamin C2 temporally coincides with that of structural protein components of another meiosis-specific karyoskeletal structure, the synaptonemal complex (SC) [11].
• This synaptonemal complex-associated DNA, isolated by proteinase digestion and phenol extraction of purified DNase-treated synaptonemal complexes, and cloned in plasmid vector pEMBL18, has a length distribution of 50-500 bp [12].
• The lysine-rich histones, particularly that one unique to meiotic cells, may through their interactions play a crucial role in SC structure [1].

Analytical, diagnostic and therapeutic context of Sycp1

• It was found that a silver-staining component of the synaptonemal complex is not grossly different from that in pachytene nuclei not subjected to digestion and extraction [13].
• In this article, we describe a new method of obtaining SC preparations for electron microscopy, as well as the results of a study of the first meiotic prophase in oocytes and spermatocytes of the rat (Rattus norvegicus Sprague Dawley) in which we analysed how the methodology used can influence the results [14].
• Although the evolution of the SCs and their related annexed structures, such as nucleoli, has been well established, sometimes it is difficult to assess whether the abnormal features observed correspond to genotoxic effects or to an artefact related to the method used to obtain the SC preparations [14].
• The somatically variable and nonargentophilic secondary constriction in the 1q arm was evident as a distinct silver-stained thickening along the synaptonemal complex [15].
• The novel application of scanning electron microscopy to study whole-mount surface-spread synaptonemal complex complements of rye (Secale cereale) and rat (Rattus norvegicus) is described [16].

References