Chromosomal complements of five species of Indian mammals

The chromosomal complements of five species of mammals, Mus musculus (Linn.), Rattus rattus rattus (Linn.), Bandicota bengalensis (Gray and Hardw.), Funambulus pennanti (Wr.) and Lepus ruficaudatus (Geoff.) were elaborated. The karyotypes of all the species were compared. The diploid number (2n) in Mus is 40, Rattus 42, Bandicota 42, Funambulus 54 and Lepus 48. An extra large X-chromosome was observed in one population of male Rattus rattus rattus (Linn.), which might have been formed as a result of duplication of the terminal segments of both the arms of the chromosomes.     

Histochemical demonstration of certain testicular enzymes of the Indian desert gerbil Meriones hurrianae jerdon and their response to unilateral cryptorchidism

Summary Active male gerbils were rendered unilaterally cryptorchid and the enzymatic changes were studied after 48, 60 and 100 days. The histochemical observations revealed inhibition of alkaline phosphatase, acid phosphatase, 5-nucleotidase, adenosine-tri-phosphatase and succinic dehydrogenase activities in the germinal elements of the seminiferous tubules. The non-specific esterase and succinic dehydrogenase activities increased in the Leydig cells to certain extent. The sudanophilic lipids increased in the Sertoli cells and the interstitial cells. An attempt has been made to approach the intricate problem of the spermatogenesis in order to understand the sequence of certain enzymatic activities in the gerbil testis in which spermatogenesis is suppressed when one of the testes is lodged inside the abdominal cavity.     

Analysis of Multimerin 1 (MMRN1) expression in ovarian cancer

Molecular Biology Reports - Ovarian cancer, the most lethal gynecological cancer, is the fifth most common cause of cancer-related deaths in women. A cost-effective and non-invasive early screening...     

First example of mixed azoheterocycles: structural studies of metallo-macrocycle Ag(I) versus tetrahedral Cd(II) complexes of pyridyl-azo-imidazole

Imidazolyl and 3^′-pyridyl are linked by azo bond (-NN-) to synthesize hitherto unknown mixed heterocyclic azo molecules, 2-[(3^′-pyridyl)azo]imidazole (3^′-PyaiH). Alkylation in presence of NaH has synthesized 1-alkyl-2-[(3^′-pyridyl)azo]imidazole (3^′-PyaiR^′). 3^′-PyaiR^′ include three types of N-donor centers: N(imidazole), N(azo) and a peripheral N(pyridine). They bind to Ag⁺ to form 2:2 metallo-macrocycle, [Ag(3^′-PyaiR^′)]₂²⁺, while the reaction with Cd²⁺ forms Cd(3^′-PyaiR^′)₄²⁺. The complexes are structurally characterized by X-ray diffraction studies.     

Cotargeting Polo-Like Kinase 1 and the Wnt/β-Catenin Signaling Pathway in Castration-Resistant Prostate Cancer

The Wnt/β-catenin signaling pathway has been identified as one of the predominantly upregulated pathways in castration-resistant prostate cancer (CRPC). However, whether targeting the β-catenin pathway will prove effective as a CRPC treatment remains unknown. Polo-like kinase 1 (Plk1) is a critical regulator in many cell cycle events, and its level is significantly elevated upon castration of mice carrying xenograft prostate tumors. Indeed, inhibition of Plk1 has been shown to inhibit tumor growth in several in vivo studies. Here, we show that Plk1 is a negative regulator of Wnt/β-catenin signaling. Plk1 inhibition or depletion enhances the level of cytosolic and nuclear β-catenin in human prostate cancer cells. Furthermore, inhibition of Wnt/β-catenin signaling significantly potentiates the antineoplastic activity of the Plk1 inhibitor BI2536 in both cultured prostate cancer cells and CRPC xenograft tumors. Mechanistically, axin2, a negative regulator of the β-catenin pathway, serves as a substrate of Plk1, and Plk1 phosphorylation of axin2 facilitates the degradation of β-catenin by enhancing binding between glycogen synthase kinase 3β (GSK3β) and β-catenin. Plk1-phosphorylated axin2 also exhibits resistance to Cdc20-mediated degradation. Overall, this study identifies a novel Plk1-Wnt signaling axis in prostate cancer, offering a promising new therapeutic option to treat CRPC.