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I struggled between those two answer choices as well. I thought that the large needle shape right in the middle was a uric acid crystal which helped push me towards Uric Acid as my answer. I also took into account that she was older (even though STIs are rampant among the elderly) she didn't really seem to have any other symptoms or history of STI/gonorrhea. I figured with her age that she just wasn't able to excrete Uric Acid enough, and got a gout.
Something a pathologist told me one time was that they put the focus of the picture in the middle of the shot. So considering the uric acid-looking shape was right in the middle, I figured that's what they wanted us to focus on with the picture.
Hope this helps.
Ah gotcha! I guess I shouldn't have thought that the thing in the middle was an artifact lol... thank you!!
I believe it's because:
1) there is nothing given that would be risk factors for this woman to have N. gonorrhea
2) The thing in the middle is indeed an MSU crystal, just not under polarized light
3) apparently we get acute inflammation and increase in WBCs with crystal-induced arthropathies, per Table 11-2 on page 8 here (10 page document, top of page of interest will say p. 260) --> http://downloads.lww.com/wolterskluwer_vitalstream_com/sample-content/9781582558752_Mundt/samples/Chapter_11.pdf Also take a look at the pics on the previous page, left column for an example.
I got this wrong as well, but I definitely won't again! lol
i had the same problem, Whats about the fever?, could be present in gout?
I think this question mentioned the patient's temp was 100.4 which is consistent with mild fever in gout from inflammation.
This photo was wack though
The damage in gout is mediated by Neutrophils, so makes complete sense you see a bunch.
why not membrane receptor?
delF508 is a 3 base pair deletion of phenylalanine at amino acid position 508. Mutation causes impaired post-translational processing of CFTR (improper folding) which rough ER detects. Sends mutant misfolded CFTR to the proteasome for degradation, preventing it from reaching cell surface. So problem is not malfunctioning CFTR channels in the surface; problem is complete absence of CFTR on cell surface (since they keep getting misfolded and sent to proteasome to be trashed). Source of primary problem: error in protein structure
@Is3076 because the CFTR is a channel not a receptor.
FA 2019 p. 60
@a1913 is correct- as for @angelaq11, you can still have a receptor that also functions as a channel as they are not mutually exclusive. An example of this is the nAChR found on postsynaptic NMJ neurons. This is a non-selective, ligand-gated, ionotropic receptor that functions as a channel once its ligand (i.e., ACh) has bound to the active site to induce conformational change. Similarly on the same realm: CFTR is an ionotropic receptor that concurrently functions as a Cl- channel once its ligands (ie. 2 ATP) is bound to open the channel and enable Cl- flux.
This question in particular is asking for the underlying pathophysiologic mechanism for cystic fibrosis, which boils down to an issue with the primary structure of a protein resulting in its misfolding and subsequent sequestration/degradation.