Latar belakang: Voltage dependent anion channel (VDAC) merupakan protein spesifi k yang memperantarai transport anion, kation dan ATP dan berperan penting pada motilitas sperma. Penelitian ini bertujuan mengevaluasi pengaruh antibody VDAC3 poliklonal terhadap motilitas sperma manusia. Metode: Antibodi VDAC3 poliklonal diproduksi dengan mengimunisasi kelinci dengan peptid sintetik spesifi k VDAC3. Serum kelinci sebelum diimunisasi dikoleksi menjadi preimunserum untuk kontrol percobaan. Pengenalan antiserum VDAC3 yang diproduksi terhadap antigen VDAC3 pada sperma dilakukan dengan menggunakan metode western blot. Sperma dengan motilitas baik dari 30 pria fertile dicuci dan diisolasi dengan menggunakan metode Percoll gradient. Evaluasi pengaruh antibody VDAC3 terhadap motilitas sperma dilakukan dengan mengukur kecepatan gerak sperma (detik/0,1 mm) dan menghitung jumlah sperma tidak bergerak (juta/ml) pada 0 menit, 30 menit, 60 menit setelah penambahan antiserum dan preimunserum. Data kecepatan sperma dan jumlah sperma tidak bergerak dianalisis dengan mengunakan program statistic SPSS 13.0. Hasil: Antiserum VDAC3 dapat mengenali protein VDAC3 pada sperma dan dapat meningkatkan jumlah sperma tidak bergerak setelah 60 menit secara bermakna dibandingkan preimunserum. Kecepatan gerak sperma menurun secara bermakna setelah penambahan antiserum VDAC3 pada menit ke 0, 30 dan 60 dibandingkan dengan preimunserum.

AbstrakTelah dilakukan penelitian tentang efek pemberian kombinasi testosteron undekanoat (TU)

Background: Androgen deprivation therapy (ADT) is a standard treatment for advanced prostate cancer (PCa). However, PCa recurrence and progression rates during ADT are high. Until now, there has been no evidence regarding when progression begins. This study evaluated the gene expression of intraprostatic androgen receptor (AR) and steroidogenic enzymes in the early stages of ADT. Methods: Prostate tissue samples were taken from PCa patients with urinary retention who received ADT (ADT-PCa; n=10) and were further subgrouped into ADT ≤12 months (n=4) and ADT >12 months (n=6). The ADT-PCa tissues were then compared with BPH (n=12) and primary (no treatment) PCa tissues (n=16). mRNA for gene expression analysis of AR and steroidogenic enzymes was extracted from formalin-fixed paraffin embedded (FFPE) tissues and analyzed by real-time PCR. Protein expression was evaluated by immunohistochemistry with specific antibodies. Results: AR gene expression was higher in the ADT-PCa group than in the BPH or primary PCa group. Both the ADT ≤12 and > 12 months subgroups had significantly higher relative gene expression levels of AR (p<0.01 and 0.03, respectively) than the primary PCa group. In the ADT-PCa group, AR protein expression showed an increasing trend in the ADT ≤12 months subgroup and was significantly elevated in the ADT >12 months subgroup compared with the PCa group (100%; p <0.01). Half (50%) of the patients in the ADT ≤12 months subgroup were found to have upregulation of AR, and one showed upregulation beginning at 3 months of ADT. A trend toward elevated relative gene expression of SRD5A3 was also apparent in the ADT groups. Conclusion: AR and steroidogenic enzymes are upregulated in ADT-PCa patients as early as 3 months, without PSA elevation. Steroidogenic enzymes, particularly SRD5A3, were also upregulated before PSA rose.

No abstract

MMP-9 overexpression is associated with a poor outcome in MDR-TB patients, indicating that MMP-9 is a suitable target for MDR-TB therapy. MMP-9 also includes SNPs that occur at inhibitor binding areas as well as zinc ions. As a result of polymorphisms, the usage of MMP-9 inhibitors for MDR-TB might vary. Through molecular simulation, it has been found that the mutant MMP-9 has a larger cavity and a more lipophilic surface. The docking tests revealed that EGTA had the least amount of binding energy to both wild-type and mutant MMP-9. The wildtype MMP-9 can bind zinc when EGTA is in the active site. This shows that using EGTA to chelate Zn is only partially successful. However, the binding energy of EGTA at the active site suggests that it may be a competitor to MMP-9 substrates. On the other hand, Zn is not involved in the interaction of the mutant MMP-9-EGTA complex.