This blog is devoted to BIOL 6988, a graduate level seminar in the biological sciences at Youngstown State University. While targeted towards graduate students, BIOL 6988 actively incorporates undergraduate participants in their scholastic endeavors in the biological sciences. This blog is intended as a educational tool not just for YSU students and faculty, but for anyone who wishes to contribute to an active-learning environment.
During our second seminar this semester, Dr. Walker presented his research summary titled: Myogenesis: Quantitative PCR Approach to Studying Muscle Development and Expression of Myosin Heavy Chain and Titin. The assembly of the sarcomere is controlled by the expression of particular genes at specific times during growth of muscle cells. These targets genes, six in total, were mainly on myosin heavy chain and specific sarcomeric markers. The myosin heavy chain target genes and the titin isoforms increased after confluency had occurred. Do you think actin isoform expression would act similarly to myosin and titin during cell development?
I enjoyed Dr. Walkers presentation, and I thought it was interesting to learn of his back story. I think it's interesting to hear of how my instructors ended up where they are today and to see that life is full of curveballs.
In relaiton to Hillari's question, I would think it is safe to assume they undergo a similiar developmental process since they are both part of skeletal muscle within the muscle fibers. Actin would be developing closely with myosin and titin during the cell develope because they must fuction together properly for a muscle to contract. I would think actin would undergo a slightly different developement because it does severe a different purpose within the muscle fiber than myosin and titin does.
I enjoyed Dr. Walker's presentation and the inclusion of his academic journey. I was surprised when he said that his favorite place he's been thus far is Pittsburgh.
In reference to Hillari's question, I agree with Anna. Being that actin is a muscular filament, I feel as though it would act somewhat similarly to myosin and titin. I would assume there will be small differences between all three but they will also share several similarities.
I was glad to hear that Dr. Walker went to The University of Miami, which is in my hometown. I was quite interested when he mentioned his work with 'cell printing.'
Now to answer Hillaris question on how actin isoform expression acts similarly to Myosin and Titin during muscle development, I would assume that actin would interact more with Titin than with Myosin. Myosin is attached to the z line, where as Myosin attaches directly to Titin, which in turn provides the scaffolding for development.
I have seen a couple of Dr. Walker's talks and worked with him in his lab, but I had never heard his story like that before. How can we possibly know where we might end up? I have always thought his research was quite intriguing, and I like that he works with mammalian cells.
As for Hillari's question, I know that actin has a lot of roles in cytoskeletal structure in general. However, I would not be surprised at all to find that the actin isoforms found in muscle cells can be specialized and quite distinct. Therefore, I would expect that the differential expression of these actin isoforms could very well influence cell development.
I also agree with Anna. During cell development I would imagine that actin isoform expression would act similarly to both myosin and titin. As they are all closely involved in muscle contraction. Because this is in a developmental state however, there may be slightly different interactions going on.
I enjoyed the way Dr. Walker started the seminar with his academic journey and what led him to his current research area.
Actin and myosin are proteins that interact in an organized function to bring about muscle contraction. While actin is a long thin filament, myosin is thick with heads and tails. Like Anna and Jessica mentioned, i believe actin isoform's development would be similar to myosin and titin to some extent due to their functions.There would be a slight difference due to their structures.
I enjoyed being able to hear about Dr. Walker's journey during his talk and his research was very interesting to listen to as well.
For Hillari's question, I would also agree with Anna. Since actin is also a part of the skeletal muscle in muscle fibers, they are all required for muscle contraction and all interact with one another. There may be a few differences between them and actin, but overall they would act very similar during cell development.
First off, I liked Dr. Walker's take on the presentation, as he showed how he got to the spot where he is today. It is interesting to see what he did and how it compares to what I am currently doing. As for the question, I would imagine that actin would similarly be expressed as myosin and titin would, as actin is a necessary part of myofibrils. Feeling curious, I found an article on pubmed that from the abstract said that in C2C12, cardiac actin is the major gene product during differentiation. In adult skeletal muscles α-skeletal actin is the major gene product however, possibly meaning that cardiac actin is somehow necessary for development. The article: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC368933/pdf/molcellb00150-0029.pdf
I really enjoyed hearing about Dr. Walker's past and all the influential people that he has encountered and worked with. As for the question that Hillari asked, I, too, think that the actin isoform expression would act similarly to myosin and titin during cell development, since actin interdigitates with myosin in the sarcomere. I do think there would be developmental differences, but it seems like the expression would be similar in order to produce the well-organized sarcomere in the end.
I enjoyed Dr. Walker presentation on the journey throughout his academic life and the current research on myogenesis and the expression of myosin heavy chain and titin isoform. myogenesis involves the sequential change in myogenic genes. Titin is known as a long flexible protein in striated muscles that is assumed to be responsible for passive tension generated upon stretch. Titin filaments are believed to link myosin filament to Z-band. On Hillari's question i could say there is similarity on action isoform expression reaction and myosin and titin during cell development.
I learned a lot about Dr. Walker during his talk, and was interested to hear of his background and everywhere he has been. I think it really speaks to the students to see where they started and how they ended up where they are today. I would say there is a similarity between the actin, myosin, and titin expressions in creating muscle. The thin filaments of a muscle are composed of actin, troponin and tropomyosin. Actin is also a protein that forms a double helix. Alpha actinin helps form the Z-line and also anchors the thin filaments. Titin helps resist overstretching of the muscle. It generates enough tension to prevent this overstretching
Hey everyone,
ReplyDeleteDuring our second seminar this semester, Dr. Walker presented his research summary titled: Myogenesis: Quantitative PCR Approach to Studying Muscle Development and Expression of Myosin Heavy Chain and Titin. The assembly of the sarcomere is controlled by the expression of particular genes at specific times during growth of muscle cells. These targets genes, six in total, were mainly on myosin heavy chain and specific sarcomeric markers. The myosin heavy chain target genes and the titin isoforms increased after confluency had occurred. Do you think actin isoform expression would act similarly to myosin and titin during cell development?
I enjoyed Dr. Walkers presentation, and I thought it was interesting to learn of his back story. I think it's interesting to hear of how my instructors ended up where they are today and to see that life is full of curveballs.
ReplyDeleteIn relaiton to Hillari's question, I would think it is safe to assume they undergo a similiar developmental process since they are both part of skeletal muscle within the muscle fibers. Actin would be developing closely with myosin and titin during the cell develope because they must fuction together properly for a muscle to contract. I would think actin would undergo a slightly different developement because it does severe a different purpose within the muscle fiber than myosin and titin does.
I enjoyed Dr. Walker's presentation and the inclusion of his academic journey. I was surprised when he said that his favorite place he's been thus far is Pittsburgh.
ReplyDeleteIn reference to Hillari's question, I agree with Anna. Being that actin is a muscular filament, I feel as though it would act somewhat similarly to myosin and titin. I would assume there will be small differences between all three but they will also share several similarities.
I was glad to hear that Dr. Walker went to The University of Miami, which is in my hometown. I was quite interested when he mentioned his work with 'cell printing.'
ReplyDeleteNow to answer Hillaris question on how actin isoform expression acts similarly to Myosin and Titin during muscle development, I would assume that actin would interact more with Titin than with Myosin. Myosin is attached to the z line, where as Myosin attaches directly to Titin, which in turn provides the scaffolding for development.
I have seen a couple of Dr. Walker's talks and worked with him in his lab, but I had never heard his story like that before. How can we possibly know where we might end up?
ReplyDeleteI have always thought his research was quite intriguing, and I like that he works with mammalian cells.
As for Hillari's question, I know that actin has a lot of roles in cytoskeletal structure in general. However, I would not be surprised at all to find that the actin isoforms found in muscle cells can be specialized and quite distinct. Therefore, I would expect that the differential expression of these actin isoforms could very well influence cell development.
I also agree with Anna. During cell development I would imagine that actin isoform expression would act similarly to both myosin and titin. As they are all closely involved in muscle contraction. Because this is in a developmental state however, there may be slightly different interactions going on.
ReplyDeleteI enjoyed the way Dr. Walker started the seminar with his academic journey and what led him to his current research area.
ReplyDeleteActin and myosin are proteins that interact in an organized function to bring about muscle contraction. While actin is a long thin filament, myosin is thick with heads and tails. Like Anna and Jessica mentioned, i believe actin isoform's development would be similar to myosin and titin to some extent due to their functions.There would be a slight difference due to their structures.
I enjoyed being able to hear about Dr. Walker's journey during his talk and his research was very interesting to listen to as well.
ReplyDeleteFor Hillari's question, I would also agree with Anna. Since actin is also a part of the skeletal muscle in muscle fibers, they are all required for muscle contraction and all interact with one another. There may be a few differences between them and actin, but overall they would act very similar during cell development.
First off, I liked Dr. Walker's take on the presentation, as he showed how he got to the spot where he is today. It is interesting to see what he did and how it compares to what I am currently doing. As for the question, I would imagine that actin would similarly be expressed as myosin and titin would, as actin is a necessary part of myofibrils. Feeling curious, I found an article on pubmed that from the abstract said that in C2C12, cardiac actin is the major gene product during differentiation. In adult skeletal muscles α-skeletal actin is the major gene product however, possibly meaning that cardiac actin is somehow necessary for development. The article: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC368933/pdf/molcellb00150-0029.pdf
ReplyDeleteThis comment has been removed by the author.
ReplyDeleteI really enjoyed hearing about Dr. Walker's past and all the influential people that he has encountered and worked with. As for the question that Hillari asked, I, too, think that the actin isoform expression would act similarly to myosin and titin during cell development, since actin interdigitates with myosin in the sarcomere. I do think there would be developmental differences, but it seems like the expression would be similar in order to produce the well-organized sarcomere in the end.
ReplyDeleteI enjoyed Dr. Walker presentation on the journey throughout his academic life and the current research on myogenesis and the expression of myosin heavy chain and titin isoform.
ReplyDeletemyogenesis involves the sequential change in myogenic genes. Titin is known as a long flexible protein in striated muscles that is assumed to be responsible for passive tension generated upon stretch. Titin filaments are believed to link myosin filament to Z-band. On Hillari's question i could say there is similarity on action isoform expression reaction and myosin and titin during cell development.
I learned a lot about Dr. Walker during his talk, and was interested to hear of his background and everywhere he has been. I think it really speaks to the students to see where they started and how they ended up where they are today.
ReplyDeleteI would say there is a similarity between the actin, myosin, and titin expressions in creating muscle. The thin filaments of a muscle are composed of actin, troponin and tropomyosin. Actin is also a protein that forms a double helix. Alpha actinin helps form the Z-line and also anchors the thin filaments. Titin helps resist overstretching of the muscle. It generates enough tension to prevent this overstretching