scholarly journals The Content of Low Density Lipoprotein, High Density Lipoproteins, Cholesterol on Pen Shells (Atrina Pectinata) Fish Catch in Kenjeran Surabaya

2020 ◽  
Vol 7 (2) ◽  
pp. 51
Author(s):  
Rio Khalif Eldiaz ◽  
Agustono Agustono ◽  
Kustiawan Tri Pursetyo

Pen Shells (A. pectinata) Is one type of a clam that is mostly consumed, Cholesterol levels included in a category high. Although the high cholesterol levels. Shells also contain levels commonly called ldl cholesterol evil . Having shells also levels of hdl, Cholesterol levels total normal in plasma adults is of 120 until 200 mg/dl. Different from its function at the time of cholesterol levels normal, the higher cholesterol levels in the blood, the greater the risk of atherosclerosis also. The purpose of this research is to get information about ldl levels , hdl and cholesterol contained in shells kampak , as well as to determine the shells kampak who most worthy for consumption. Parameter that observed in this research was ldl , hdl , cholesterol .This study using methods descriptive against the difference levels of low density lipopprotein ( ldl ) and high-density lipoproteins ( hdl ) and cholesterol in any bivalve hatchets the results of catch fishermen in kenjeran surabaya. Average levels of ldl on pen shells (A. pictinata) In the meat is 30,990 mg/100g, in the muscle is 28,329 mg/100g and in the Digestive organs is 25,225 mg/100g ; The average levels of hdl on pen shells (A. pictinata) in the meat is 96,772 mg/100g, in the muscle is 87,139 mg/100g and in the Digestive organs is 67,516 mg/100g ; average levels of cholesterol on pen shells (A. pictinata) in the meat is 165,609 mg/100g, in the muscle is 147,382 mg/100g and in the Digestive organs is 114,551 mg/100g. Levels of LDL, HDL and cholesterol Lead to results same that is the most number are located on the meat, then muscle and at least there are on an disgestive organ.

2014 ◽  
Vol 1 (2) ◽  
Author(s):  
Defitson Adolfo Gopdianto

AbstractBackground: Decrease or increase in blood HDL cholesterol levels affect smokers and nonsmokers. Cigarettes have chemicals that can lead to several health problems such as nicotine. Nicotine resulted in the production of very low density lipoprotein(VLDL) in order to reduce redundant high density lipoprotein cholesterol levels.Method: This type of researchis anobservationalstudyusing across sectional design. Thisstudy populationisstudents ofthe Faculty ofMedicine, University ofSamRatulangi7th semesterof the school year2012/2013with apopulation of150people. Sampling technique inthis research is byusingpurposivesamplingtechniques, smokersand nonsmokersobtainedusing a questionnaire.Result: Determinedthatthere is astatisticallysignificant differencebetweenHDLcholesterol levelsin theblood ofmalesmokersand nonsmokersp=0.49.Cinclusion: There isstatistically significantdifferences inHDLcholesterol levelsin theblood ofmalesmokersand nonsmokers.Keywords: HDLcholesterol levels, smokers, and nonsmokersAbstrakLatar belakang: Penurunan atau peningkatan kadar kolesterol HDL darah berpengaruh pada perokok dan bukan perokok. Rokok memiliki bahan-bahan kimiawi yang dapat mengakibatkan beberapa gangguan kesehatan diantaranya adalah nikotin. Nicotineresulted inthe production ofvery low densitylipoprotein(VLDL) in order toreduceexcessivelevels ofhigh densitylipoproteincholesterol.Metode: Jenis penelitian merupakan penelitian observasional dengan menggunakan rancangan cross sectional.Populasi penelitian ini yaitu mahasiswa Fakultas Kedokteran Universitas Sam Ratulangi semester 7 tahun ajaran 2012/2013 dengan besar populasi berjumlah 150 orang. Teknik pengambilan sampel pada penelitian ini yaitu dengan menggunakan teknik purposive sampling, perokok dan bukan perokok didapatkan dengan menggunakan kuesioner.Hasil:Secara statistik ditetapkan bahwa terdapat perbedaan yang bermakna antara kadar kolesterol HDL darah pada pria perokok dan bukan perokok p=0,49.Kesimpulan: Secara statistik ada perbedaan kadar kolesterol HDL darah pada pria perokok dan bukan perokok.Kata kunci: Kadar kolesterol HDL, perokok, dan bukan perokok.


1980 ◽  
Vol 26 (9) ◽  
pp. 1261-1265 ◽  
Author(s):  
J Gabor ◽  
M Spain ◽  
N Kalant

Abstract We examined the cholesterol/protein ratio and the apoprotein composition of serum lipoproteins in a randomly selected population of maturity-onset diabetics and in a group of nondiabetics of similar age. We found no differences in cholesterol distribution between the groups as a whole, but diabetics with above-normal low-density lipoproteins (LDL) had decreased concentrations of high-density lipoprotein (HDL) cholesterol. In the diabetics as a whole, there was an increase in the cholesterol/protein ratio in HDL, a negative correlation between the amounts of LDL cholesterol and HDL cholesterol, an increase in the proportion of apolipoprotein C in very-low-density lipoprotein (VLDL), and a decrease in the proportion of the apolipoprotein AI component of HDL. In diabetic subjects with increased VLDL, there was an increase in the relative amount of apolipoprotein CIII, and a consequent decrease in the ratio of apolipoprotein CII/apolipoprotein CIII in the VLDL. In both diabetic and control subjects, apolipoprotein E and cholesterol content of VLDL were linearly related.


1987 ◽  
Vol 65 (3) ◽  
pp. 252-260 ◽  
Author(s):  
S. P. Tam ◽  
W. C. Breckenridge

The nature of the interaction of high density lipoproteins (HDL), formed during lipolysis of human very low density lipoprotein (VLDL) by perfused rat heart, with subfractions of human plasma HDL was investigated. Perfusate HDL, containing apoliproproteins (apo) E, C-II, and C-III but no apo A-I or A-II, was incubated with a subfraction of HDL (HDL-A) containing apo A-I and A-II, but devoid of apo C-II, C-III, and E. The products of the incubation were resolved by heparin-Sepharose or hydroxylapatite chromatography under conditions which allowed the resolution of the initial HDL-A and perfusate HDL. The fractions were analyzed for apolipoprotein content and lipid composition and assessed for particle size by electron microscopy. Following the incubation, the apo-E-containing lipoproteins were distinct from perfusate HDL since they contained apo A-I as a major component and apo C-II and C-III in reduced proportions. However, the HDL-A fraction contained apo C-II and C-III as major constituents. Associated with these changes in apolipoprotein composition, the apo-E-rich lipoproteins acquired cholesteryl ester from the HDL-A fraction and lost phospholipid to the HDL-A fraction. The HDL-A fraction maintained a low unesterified cholesterol/phospholipid molar ratio (0.23), while the apo-E-containing lipoproteins possessed a high ratio (0.75) characteristic of the perfusate HDL. The particle size of apo-E-containing lipoproteins (138.9 ± 22.5 Å; 1 Å = 0.1 nm) was larger than the initial HDL-A (126.5 ± 17.6 Å) or the new HDL-A-like fraction (120.9 ± 17.4 Å) obtained following incubation with perfusate HDL. It is concluded that incubation of perfusate HDL containing apo E, C-II, and C-III with plasma HDL subfractions results in the acquisition of apo A-I and cholesteryl esters by the apo-E-containing perfusate HDL and the loss of apo C-II, C-III, and phospholipid to the plasma HDL-A fraction. The process does not appear to be due to fusion of the particles, since the apo-E-containing lipoproteins maintain a cholesterol/phospholipid ratio distinct from the HDL-A fraction. The data provide evidence for a potential mechanism for the formation of HDL-E, an apo-E-containing lipoprotein of HDL size and density, through lipolysis of VLDL.


1985 ◽  
Vol 226 (3) ◽  
pp. 715-721 ◽  
Author(s):  
F M Van't Hooft ◽  
A Van Tol

O-(4-Diazo-3-[125I]iodobenzoyl)sucrose ([125I]DIBS), a novel labelling compound specifically designed to study the catabolic sites of serum proteins [De Jong, Bouma, & Gruber (1981) Biochem. J. 198, 45-51], was applied to study the tissue sites of degradation of serum lipoproteins. [125I]DIBS-labelled apolipoproteins (apo) E and A-I, added in tracer amounts to rat serum, associate with high-density lipoproteins (HDL) just like conventionally iodinated apo E and A-I. No difference is observed between the serum decays of chromatographically isolated [125I]DIBS-labelled and conventionally iodinated HDL labelled specifically in either apo E or apo A-I. When these specifically labelled HDLs are injected into fasted rats, a substantial [125I]DIBS-dependent 125I accumulation occurs in the kidneys and in the liver. No [125I]DIBS-dependent accumulation is observed in the kidneys after injection of labelled asialofetuin or human low-density lipoprotein. It is concluded that the kidneys and the liver are important sites of catabolism of rat HDL apo E and A-I.


2003 ◽  
Vol 47 (9) ◽  
pp. 2796-2803 ◽  
Author(s):  
Kishor M. Wasan ◽  
Olena Sivak ◽  
Richard A. Cote ◽  
Aaron I. MacInnes ◽  
Kathy D. Boulanger ◽  
...  

ABSTRACT The objective of this study was to determine the distribution profile of the novel endotoxin antagonist E5564 in plasma obtained from fasted human subjects with various lipid concentrations. Radiolabeled E5564 at 1 μM was incubated in fasted plasma from seven human subjects with various total cholesterol (TC) and triglyceride (TG) concentrations for 0.5 to 6 h at 37°C. Following these incubations, plasma samples were separated into their lipoprotein and lipoprotein-deficient fractions by ultracentrifugation and were assayed for E5564 radioactivity. TC, TG, and protein concentrations in each fraction were determined by enzymatic assays. Lipoprotein surface charge within control and phosphatidylinositol-treated plasma and E5564’s influence on cholesteryl ester transfer protein (CETP) transfer activity were also determined. We observed that the majority of E5564 was recovered in the high-density lipoprotein (HDL) fraction. We further observed that incubation in plasma with increased levels of TG-rich lipoprotein (TRL) lipid (TC and TG) concentrations resulted in a significant increase in the percentage of E5564 recovered in the TRL fraction. In further experiments, E5564 was preincubated in human TRL. Then, these mixtures were incubated in hypolipidemic human plasma for 0.5 and 6 h at 37°C. Preincubation of E5564 in purified TRL prior to incubation in human plasma resulted in a significant decrease in the percentage of drug recovered in the HDL fraction and an increase in the percentage of drug recovered in the TRL and low-density lipoprotein fractions. These findings suggest that the majority of the drug binds to HDLs. Preincubation of E5564 in TRL prior to incubation in normolipidemic plasma significantly decreased the percentage of drug recovered in the HDL fraction. Modifications to the lipoprotein negative charge did not alter the E5564 concentration in the HDL fraction. In addition, E5564 does not influence CETP-mediated transfer activity. Information from these studies could be used to help identify the possible components of lipoproteins which influence the interaction of E5564 with specific lipoprotein particles.


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