Serum protein electrophoresis (EPH) is used to assess relative concentrations of blood proteins in clinical and biological studies. Serum EPH fractions have been determined for elasmobranchs using mammalian albumin, alpha 1‐, alpha 2‐, beta‐, and gamma‐globulin fractions, and have been deemed fractions 1 through 5, respectively. However, serum EPH fraction concentration reference intervals (RIs) have not been widely established for different elasmobranch species. In this study, RIs for fractions 1 through 5 were determined from 45 wild‐caught Nurse Sharks Ginglymostoma cirratum (27 females and 23 males) in South Florida. Serum samples were isolated from whole blood following caudal venipuncture. Body condition was also measured in the field to assess the relative health of the individuals sampled. There was no relationship between body condition and serum EPH fraction concentrations. In addition, there was no difference in body condition or serum EPH fraction concentrations between females and males. Total solids and total protein values were significantly different (P < 0.001). Nurse Shark serum EPH fraction 1 was found within the mammalian albumin migrating band distance and was negligible. Fraction 2 showed no peak in the mammalian alpha 1‐globulin range. A thin, medium peak in the mammalian alpha 2‐globulin range represented fraction 3. In the mammalian beta‐globulin range, fraction 4 consisted of the majority of protein observed. It was represented by a smooth, broad peak. A short, medium broad peak in the mammalian gamma‐globulin range represented fraction 5. The Nurse Shark serum EPH fraction RIs provided in this study may be utilized to clinically evaluate the health of Nurse Sharks in captivity and in the wild, and to compare the health of their populations around the world experiencing various anthropogenic stressors and other environmental impacts.
Reported here are the relationships among morphological (i.e., body condition) and biochemical (i.e., plasma concentrations of triglycerides, cholesterol, free fatty acids, and ketone bodies and ketone body ratios) parameters related to energy storage and use, as well as the variation of such parameters, for 107 freeranging nurse sharks Ginglymostoma cirratum sampled off South Florida. Immature G. cirratum exhibited a higher variance in body condition, plasma free fatty acid concentrations and ketone body ratios compared to adults. Mature female G. cirratum had significantly higher body condition than mature males, driven by a seasonal increase in mature female body condition during the wet season. Mature male G. cirratum showed a decrease in the ketone body β-hydroxybutyric acid during the dry season. Taken together, this study provides a baseline assessment of body condition and internal physiological state for a data-poor marine species and demonstrates significant ontogenetic, sexual and seasonal variation in G. cirratum energetic state. As concluded by other studies of energy metabolism in free-ranging sharks, this research highlights the importance of considering intraspecific patterns and sampling context for inferring the drivers of variation.
Serum proteins found in the blood have been used as diagnostic markers in both human and animal medicine. Evaluating proteins in the blood of sharks may be a valuable way to assess shark health. The purpose of this study was to perform serum protein electrophoresis from non-lethal blood samples of wild sharks and establish baseline values for six species off South Florida: blacknose (Carcharhinus acronotus), blacktip (Carcharhinus limbatus), bull (Carcharhinus leucas), lemon (Negaprion brevirostris), sandbar (Carcharhinus plumbeus), and tiger shark (Galeocerdo cuvier). Two hundred and fifty-one serum samples were collected between 2015-2018 along with sex determination and morphometric measurements. Agarose gel analysis was performed using mammalian protein fraction delimits albumin, alpha 1-globulins, alpha 2-globulins, beta globulins, and gamma globulins alternatively defined as fractions 1-5. Reference electrophoretic profiles were established for each species, revealing the dominance of protein fractions 3 and 4. The fraction 3:4 ratio was determined for each shark and reference intervals for total solids, protein fractions, and fraction 3:4 ratio are reported for each species. There were no significant differences in total solids or protein fractions between males and females of any species. In both blacktip sharks and bull sharks, total solids was positively correlated with body size, but not in the other species evaluated. In blacknose sharks, the fraction 3:4 ratio was positively correlated with body condition. Results suggest that there may be differences in total solids values across dry and wet seasons for some species. Newly established reference intervals can now be utilized in future research to evaluate the health of captive sharks and to investigate the health status of individuals in the wild as well as relate health measures to environmental conditions.
The acute phase protein, C-reactive protein (CRP), has become an established clinical biomarker in both animal and human health, where it is used to assess the degree of acute and/or chronic inflammation. CRP has also been proposed as a potential biomarker for measuring health in sharks by indicating when a shark is experiencing an inflammatory state or is under a chronic state of stress that may have significant physiological impact. Despite the promise in using increased levels of CRP as well as other acute phase proteins as indicators of compromised health, there has not to date been a developed shark-specific assay to accurately measure CRP. An initial step in the development of a specific bioassay for CRP is isolation and characterization of the protein. The purpose of the present study is to use both field and laboratory techniques to obtain serum samples and isolate CRP from nurse sharks, Ginglymostoma cirratum. A secondary aim is to characterize the molecule and produce shark CRP specific antisera. A two step isolation procedure is now being refined to positively identify the pentraxins present and characterize them further. Protein affinity chromatography was used to identify serum amyloid P component (SAP) in addition to CRP given that they are both pentraxin proteins displaying similar binding properties. Isolated protein bands resulting from concentrated chromatographic peaks were analyzed by LC-MS/MS. Results thus far include the isolation of a pentraxin domain-containing protein within shark serum.
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