scholarly journals Short Communication: Effect of cryopreservation on ultrastructure and mitochondrial function of albino Pangasius catfish spermatozoa

2020 ◽  
Vol 21 (10) ◽  
Author(s):  
Uswatun Hasanah ◽  
ABINAWANTO ABINAWANTO ◽  
A ALIMUDDIN ◽  
Arief Boediono ◽  
Eni Kusrini
Keyword(s):  
Endangered Species ◽  
Cell Membrane ◽  
Cell Viability ◽  
Mitochondrial Function ◽  
Short Communication ◽  
Skim Milk ◽  
Storage Period ◽  
Intact Membrane ◽  
Communication Effect ◽  
Cryopreservation Techniques

Abstract. Hasanah U, Binawanto, Alimuddin A, Boediono A, Kursini E. 2020. Short Communication: Effect of cryopreservation on ultrastructure and mitochondrial function of albino Pangasius catfish spermatozoa. Biodiversitas 21: 4524-4528. Cryopreservation techniques have been carried out on many endangered species and animals with unique characteristics. Successful cryopreservation techniques vary between species depending on various factors. The study used cryopreserved spermatozoa of the albino Pangasius catfish as samples. The cryopreserved spermatozoa were analyzed by its ultrastructure, functional mitochondria, and viability. The cryopreservation was performed using a combination of 10% methanol, skim milk, and fish ringer extender. A deep freezer is used for cryopreservation at -80 °C with a storage period of 14 days. Observations were made on fresh spermatozoa, post-equilibration spermatozoa, and frozen-thaw spermatozoa. This study found there were differences in ultrastructure and morphology in the three treatments. Fresh spermatozoa and post-equilibration spermatozoa appeared intact membrane, mitochondrial, and flagellar structures. In contrast, in frozen-thaw spermatozoa, there was damage to the cell membrane. The study showed different percentages of yields on functional mitochondria of fresh spermatozoa (98 ± 2%), spermatozoa post-equilibration (57 ± 7%), frozen-thaw spermatozoa (42 ± 3.21%). Cell viability showed that there were differences in viability of fresh spermatozoa and frozen-thaw (p <0.05), the results of fresh spermatozoa (92 ± 0.57%) spermatozoa post-equilibration (80 ± 3.51%), frozen-thaw spermatozoa (61 ± 2.30%).The study concluded that the spermatozoa cryopreservation affects the ultrastructure, mitochondrial function, and viability in albino Pangasius catfish spermatozoa.

scholarly journals Changes in Particle Size, Sedimentation, and Protein Microstructure of Ultra-High-Temperature Skim Milk Considering Plasmin Concentration and Storage Temperature

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2339
Author(s):  
So-Yul Yun ◽  
Jee-Young Imm
Keyword(s):  
Particle Size ◽  
High Temperature ◽  
Storage Temperature ◽  
Whey Proteins ◽  
Skim Milk ◽  
Storage Period ◽  
Sediment Analysis ◽  
Sediment Formation ◽  
And Storage ◽  
Ultra High Temperature

Age gelation is a major quality defect in ultra-high-temperature (UHT) pasteurized milk during extended storage. Changes in plasmin (PL)-induced sedimentation were investigated during storage (23 °C and 37 °C, four weeks) of UHT skim milk treated with PL (2.5, 10, and 15 U/L). The increase in particle size and broadening of the particle size distribution of samples during storage were dependent on the PL concentration, storage period, and storage temperature. Sediment analysis indicated that elevated storage temperature accelerated protein sedimentation. The initial PL concentration was positively correlated with the amount of protein sediment in samples stored at 23 °C for four weeks (r = 0.615; p < 0.01), whereas this correlation was negative in samples stored at 37 °C for the same time (r = −0.358; p < 0.01) due to extensive proteolysis. SDS-PAGE revealed that whey proteins remained soluble over storage at 23 °C for four weeks, but they mostly disappeared from the soluble phase of PL-added samples after two weeks’ storage at 37 °C. Transmission electron micrographs of PL-containing UHT skim milk during storage at different temperatures supported the trend of sediment analysis well. Based on the Fourier transform infrared spectra of UHT skim milk stored at 23 °C for three weeks, PL-induced particle size enlargement was due to protein aggregation and the formation of intermolecular β-sheet structures, which contributed to casein destabilization, leading to sediment formation.

scholarly journals Short communication: Effect of storage and preservation on total bacterial counts determined by automated flow cytometry in bulk tank goat milk

2009 ◽  
Vol 92 (10) ◽  
pp. 4841-4845 ◽  
Author(s):  
D. Sierra ◽  
A. Sánchez ◽  
A. Contreras ◽  
C. Luengo ◽  
J.C. Corrales ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Short Communication ◽  
Goat Milk ◽  
Bacterial Counts ◽  
Bulk Tank ◽  
Communication Effect

scholarly journals Ginsenosides Rb1 and Rg1 Protect Primary Cultured Astrocytes against Oxygen-Glucose Deprivation/Reoxygenation-Induced Injury via Improving Mitochondrial Function

2019 ◽  
Vol 20 (23) ◽  
pp. 6086 ◽  
Author(s):  
Meng Xu ◽  
Qing Ma ◽  
Chunlan Fan ◽  
Xue Chen ◽  
Huiming Zhang ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Cell Viability ◽  
Mitochondrial Function ◽  
Copy Number ◽  
Glucose Deprivation ◽  
Oxygen Glucose Deprivation ◽  
Ros Production ◽  
Protective Effects ◽  
Mtdna Copy Number ◽  
Cultured Astrocytes

This study aimed to evaluate whether ginsenosides Rb1 (20-S-protopanaxadiol aglycon) and Rg1 (20-S-protopanaxatriol aglycon) have mitochondrial protective effects against oxygen-glucose deprivation/reoxygenation (OGD/R)-induced injury in primary mouse astrocytes and to explore the mechanisms involved. The OGD/R model was used to mimic the pathological process of cerebral ischemia-reperfusion in vitro. Astrocytes were treated with normal conditions, OGD/R, OGD/R plus Rb1, or OGD/R plus Rg1. Cell viability was measured to evaluate the cytotoxicity of Rb1 and Rg1. Intracellular reactive oxygen species (ROS) and catalase (CAT) were detected to evaluate oxidative stress. The mitochondrial DNA (mtDNA) copy number and mitochondrial membrane potential (MMP) were measured to evaluate mitochondrial function. The activities of the mitochondrial respiratory chain (MRC) complexes I–V and the level of cellular adenosine triphosphate (ATP) were measured to evaluate oxidative phosphorylation (OXPHOS) levels. Cell viability was significantly decreased in the OGD/R group compared to the control group. Rb1 or Rg1 administration significantly increased cell viability. Moreover, OGD/R caused a significant increase in ROS formation and, subsequently, it decreased the activity of CAT and the mtDNA copy number. At the same time, treatment with OGD/R depolarized the MMP in the astrocytes. Rb1 or Rg1 administration reduced ROS production, increased CAT activity, elevated the mtDNA content, and attenuated the MMP depolarization. In addition, Rb1 or Rg1 administration increased the activities of complexes I, II, III, and V and elevated the level of ATP, compared to those in the OGD/R groups. Rb1 and Rg1 have different chemical structures, but exert similar protective effects against astrocyte damage induced by OGD/R. The mechanism may be related to improved efficiency of mitochondrial oxidative phosphorylation and the reduction in ROS production in cultured astrocytes.

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