bioRxiv Science⌕ Search

Biology subjects

Tift, M. S.

Publications and source records attributed to Tift, M. S..

3 recordsLinked to original sources

Semi-Automated Seal Detection on the Western Antarctic Peninsula: An Unsupervised Machine Learning Approach for Detecting Ice Seals in Aerial Survey Data

Over the past 25 years, the Western Antarctic Peninsula (WAP) has experienced dramatic shifts in sea ice extent. This change has coincided with rapid alterations in ice-dependent ecosystems, including those supporting crabeater seals - the most abundant Antarctic seal and one of the largest mammalian consumers of krill. Despite their ecological importance, population estimates for ice seals remain scarce due to the difficulty of surveying large-scale, remote, ice-covered habitats. In 2023, during an abnormally low sea ice year, we conducted aerial surveys over Crystal Sound and Marguerite Bay during the end of the breeding season, flying over 1,000 km of transects. Seals were extremely sparse in the resulting imagery - occupying less than 1% of the surveyed area. This posed a significant challenge for both manual annotation and automated detection. Here we present a semi-automated, rules-based image analysis pipeline to substantially reduce human annotation time. Our method leverages hierarchical clustering with just two tunable parameters, avoiding the computational burden and opacity of deep learning models. Using this method, we identified 758 seals within a [~]350 km2 survey subset, achieving a test recall of 82%. In the absence of concurrent tagging data to estimate haul-out corrections, we refrain from extrapolating to a population estimate. However, the low observed densities highlight the urgent need for continued monitoring. Our improved data processing pipeline is a key step in facilitating the large-scale analysis required to inform conservation strategies for this key species.

ecology↗

Distribution of carbon monoxide (CO) in several tissues from Atlantic bottlenose dolphins (Tursiops truncatus)

Carbon monoxide (CO) is known as "The Silent Killer" due to its toxic effect at high concentrations, leading to an impairment in oxygen storage, delivery, and use. The cytotoxicity of CO is due to its high affinity for transition metals, such as iron, where CO outcompetes oxygen for the heme binding sites on hemoproteins in the body. CO is made in vivo in most organisms as a byproduct of heme degradation via heme oxygenase enzymes. Certain species of deep-diving marine mammals with high quantities of hemoproteins in blood and skeletal muscle have naturally elevated concentrations of CO in these tissues. To date, there exist few data on extravascular tissue CO content in wild animals. This study aims to characterize CO concentrations in nine different tissues from stranded Atlantic bottlenose dolphins (Tursiops truncatus). We found three tissues (liver, skeletal muscle, and spleen) have higher CO concentrations than other tissues. In a subset of samples from animals that tested positive for dolphin morbillivirus, the CO content in their kidney and liver was lower when compared to animals that tested negative. The mean CO concentration found in every tissue from dolphins was higher than those previously reported in healthy rodents. However, the skeletal muscle CO concentrations in dolphins from this study were much lower than those of deep-diving elephant seals. These results highlight the diversity and pattern of CO found in different tissues from bottlenose dolphins and continues to show that the heme oxygenase/carbon monoxide pathway appears to be critical for air-breathing divers.

physiology↗

Evolved increases in hemoglobin-oxygen affinity and Bohr effect coincided with the aquatic specialization of penguins.

Dive capacities of air-breathing vertebrates are dictated by onboard O2 stores, suggesting that physiological specializations of diving birds like penguins may have involved adaptive changes in convective O2 transport. It has been hypothesized that increased hemoglobin (Hb)-O2 affinity improves pulmonary O2 extraction and enhance capacities for breath-hold diving. To investigate evolved changes in Hb function associated with the aquatic specialization of penguins, we integrated comparative measurements of whole-blood and purified native Hbs with protein engineering experiments based on site-directed mutagenesis. We reconstructed and resurrected ancestral Hbs representing the common ancestor of penguins and the more ancient ancestor shared by penguins and their closest nondiving relatives (order Procellariiformes, which includes albatrosses, shearwaters, petrels, and storm petrels). These two ancestors bracket the phylogenetic interval in which penguin-specific changes in Hb function would have evolved. The experiments revealed that penguins evolved a derived increase in Hb-O2 affinity and a greatly augmented Bohr effect (reduced Hb-O2 affinity at low pH). Although an increased Hb-O2 affinity reduces the gradient for O2 diffusion from systemic capillaries to metabolizing cells, this can be compensated by a concomitant enhancement of the Bohr effect, thereby promoting O2 unloading in acidified tissues. We suggest that the evolved increase in Hb-O2 affinity in combination with the augmented Bohr effect maximizes both O2 extraction from the lungs and O2 unloading from the blood, allowing penguins to fully utilize their onboard O2 stores and maximize underwater foraging time.

evolutionary biology↗