CAMP

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Cathelicidin antimicrobial peptide precursor (18 kDa cationic antimicrobial protein) (CAP-18) (hCAP-18) [Contains: Antibacterial peptide FALL-39 (FALL-39 peptide antibiotic); Antibacterial peptide LL-37] [CAP18] [FALL39] [HSD26]

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[Study on effect of astragali radix polysaccharides in improving learning and memory functions in aged rats and its mechanism].

To observe the effect of Astragali Radix polysaccharides (APS) on the learning and memory functions of aged rats, in order to explore its mechanism for improving the learning and memory functions. Natural aging female SD rats were selected in the animal model and randomly divided into the control group, the APS low-dose group (50 mg x kg(-1)), the APS high-dose group (150 mg x kg(-1)) and the piracetam-treated group (560 mg x kg(-1)). They were orally administered with the corresponding drugs for consecutively 60 days. Besides, a young control group was set. The learning and memory functions of the rats were tested by the open-field test and the Morris water maze task. The Western-blot method was used to observe the levels of relevant neural plasticity protein N-methyl-D-aspartate receptor (NMDA receptor) in hippocampus, calcium/calmodulin dependent protein kinase II (CaMK II), protein kinase (PKA), the phosphorylation level of CAMP response element binding protein (CREB) and the protein expression of brain derived neurotrophic factor(BDNF). In this study, the authors found that the learning and memory functions and the hippocampus neural plasticity protein expression of the aged rat group were much lower than that of the young control group (P < 0.01). Compared with the aged rat group, the APS group showed the significant improvement in the impaired learning and memory functions of aged rats and the up-regulation in the hippocampus neural plasticity protein expression. The results showed that APS may improve the learning and memory functions of aged rats by increasing the expressions of relevant neural plasticity proteins.

MeSH Terms

  • Aging
  • Animals
  • Astragalus Plant
  • Brain-Derived Neurotrophic Factor
  • Cyclic AMP Response Element-Binding Protein
  • Drugs, Chinese Herbal
  • Female
  • Hippocampus
  • Humans
  • Learning
  • Memory
  • Polysaccharides
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, N-Methyl-D-Aspartate


Expression of epidermal CAMP changes in parallel with permeability barrier status.

Two critical defensive functions of the outer epidermis, the permeability barrier and antimicrobial defense, share certain structural and biochemical features. Moreover, three antimicrobial peptides (AMPs), i.e., mouse β-defensin 3 (mBD3), mouse cathelicidin antimicrobial peptide (mCAMP), and the neuroendocrine peptide, catestatin (Cst), all localize to the outer epidermis, and both mBD3 and mCAMP are secreted from the epidermal lamellar bodies with other organelle contents that subserve the permeability barrier. These three AMPs are upregulated in response to acute permeability barrier disruption, whereas conversely, mCAMP-/- mice (unable to combat Gram-positive pathogens) also display abnormal barrier homeostasis. To determine further whether these two functions are co-regulated, we investigated changes in immunostaining for these three AMPs in skin samples in which the permeability barrier function in mice had been either compromised or enhanced. Compromised or enhanced barrier function correlated with reduced or enhanced immunohistochemical expression of mCAMP, respectively, but conversely with Cst expression, likely due to the role of this AMP as an endogenous inhibitor of cathelicidin expression. mBD3 expression correlated with experimental barrier perturbations, but poorly with developmental changes in barrier function. These studies show that changes in cathelicidin and Cst expression parallel changes in permeability barrier status, with a less clear relationship with mBD3 expression.

MeSH Terms

  • Aging
  • Animals
  • Antimicrobial Cationic Peptides
  • Cathelicidins
  • Cell Membrane Permeability
  • Chromogranin A
  • Epidermis
  • Female
  • Male
  • Mice
  • Mice, Hairless
  • Mice, Knockout
  • Models, Animal
  • Peptide Fragments
  • Stress, Psychological
  • Ultraviolet Rays
  • beta-Defensins


Preparation and purification of myosin from human tracheal smooth muscle.

NaCl myosin was prepared from the annular smooth muscles of human bronchus. About 7 mg of gel filtered myosin was gained from 8 g minced tracheal muscle of the younger subject. The yield from the older (74-year old) subject was only 30% of that from the younger subject, even though the starting material was more (12 g minced tissue). Tracheal myosin contains P lipid in considerable amount; P lipids account for some 28% of the total phosphate content of the myosin, and even more (50-55%) in the case of the older subject. The preparation could be phosphorylated only in the presence of CAMP and PGF2 alpha, respectively. Cu2 treatment liberated less phosphate when compared with myosin preparations from other smooth muscles; however, the majority of the phosphate bonds underwent hydrolysis upon the effect of KOH. The reactions specific for amino acids, and also other observations allow the conclusion that the majority of covalently bound phosphate is present in an ester-type bond. Lysine-vasopressin, and also diethylpyrocarbonate successfully protect the P content of myosin from the hydrolysis inherent to incubation.

MeSH Terms

  • Adenosine Triphosphate
  • Adult
  • Aged
  • Aging
  • Chromatography, Gel
  • Humans
  • Microscopy, Electron
  • Muscle, Smooth
  • Myosins
  • Phosphates
  • Trachea


Relationships of serum plant sterols (phytosterols) and cholesterol in 595 hypercholesterolemic subjects, and familial aggregation of phytosterols, cholesterol, and premature coronary heart disease in hyperphytosterolemic probands and their first-degree relatives.

To assess relationships of serum phytosterols (plant sterols [P]) to serum cholesterol (C), P were measured by gas-liquid chromatography (GLC) in 595 hypercholesterolemics (top C quintile in screening of 3,472 self-referred subjects). A second specific aim was to determine whether high serum P would track over time and whether they would predict familial aggregation of high C, high low-density lipoprotein cholesterol (LDLC), high apolipoprotein (apo) B, and increased premature coronary heart disease (CHD) in hyperphytosterolemic probands and their first-degree relatives. Mean /- (SD) C was 260 /- 56 mg/dL, campesterol (CAMP) was 2.10 /- 1.6 micrograms/mL, stigmasterol (STIG) 1.71 /- 1.67, sitosterol (SIT) 2.98 /- 1.61, and total P 6.79 /- 3.66 micrograms/mL. Serum C correlated with CAMP (r = .15, P less than or equal to .001), STIG (r = .10, P less than or equal to .02), SIT (r = .34, P less than or equal to .0001), and total P (r = .29, P less than or equal to .0001). High serum CAMP and STIG were associated with a personal or family history of CHD in subjects less than or equal to age 55 years (premature CHD). In 21 hyperphytosterolemic probands who initially had at least one P at or above the 95th percentile and a second P at or above the 75th percentile, P were remeasured 2 years later. Initial and 2-year follow-up CAMP, STIG, and SIT did not differ (P greater than .7). Initial and follow-up CAMP were correlated (r = .47, P = .03).(ABSTRACT TRUNCATED AT 250 WORDS)

MeSH Terms

  • Aging
  • Cholesterol
  • Coronary Disease
  • Cyclic AMP
  • Female
  • Follow-Up Studies
  • Humans
  • Hyperlipoproteinemia Type II
  • Lipids
  • Lipoproteins
  • Male
  • Phytosterols
  • Sex Characteristics


Hormonal regulation of hepatic P-enolpyruvate carboxykinase (GTP) during development.

Hepatic gluconeogenesis in the rat does not begin until birth. The enzyme P-enolpyruvate carboxykinase appears initially at birth and is the final enzyme in the gluconeogenic sequence to develop. The appearance of this enzyme in the cytosol of rat liver is caused by the stimulation of enzyme synthesis, probably due directly to an increase in the hepatic concentration of cAMP. Enzyme degradation does not begin until 36 hours after birth. Studies with fetal rats in utero have shown that dibutyryl cAMP or glucagon will stimulate P-enolpyruvate carboxykinase synthesis and that this effect can be blocked by insulin. Insulin is known to depress the synthesis of P-enolpyruvate carboxykinase in adult rat liver and in Reuber H-35 liver cells in culture. The glucocorticoids are without effect on the synthesis of the enzyme in fetal rat liver. Work by Girard et al. (J. Clin. Invest. 52: 3190, 1973) has established that the molar ratio of insulin to glucagon drops from 10 immediately after birth, to 1 after one hour. This is due to both a rise in glucagon and a fall in insulin concentrations at birth. These studies, together with our work on the synthesis of P-enolpyruvate carboxykinase, indicate that the sharp drop in the concentration of insulin may relieve the normal inhibition of enzyme synthesis. This would allow the initial stimulation of enzyme synthesis by the glucagon-mediated rise in the concentration of CAMP.

MeSH Terms

  • Aging
  • Animals
  • Animals, Newborn
  • Bucladesine
  • Cytosol
  • Female
  • Fetus
  • Glucagon
  • Glucocorticoids
  • Gluconeogenesis
  • Insulin
  • Liver
  • Models, Biological
  • Phosphoenolpyruvate Carboxykinase (GTP)
  • Pregnancy
  • Rats